- INFO: Beginning work on AGXT... {November 20, 2007 11:01:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:02:30 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_AGXT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h0c.
| PDB = {{PDB2|1h0c}}, {{PDB2|1j04}}
| Name = Alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)
| HGNCid = 341
| Symbol = AGXT
| AltSymbols =; AGT; AGT1; AGXT1; PH1; SPAT; SPT; TLH6
| OMIM = 604285
| ECnumber =
| Homologene = 37251
| MGIid = 1329033
| GeneAtlas_image1 = PBB_GE_AGXT_206957_at_tn.png
| GeneAtlas_image2 = PBB_GE_AGXT_210327_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_AGXT_210326_at_tn.png
| Function = {{GNF_GO|id=GO:0004760 |text = serine-pyruvate transaminase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008453 |text = alanine-glyoxylate transaminase activity}} {{GNF_GO|id=GO:0008483 |text = transaminase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0030170 |text = pyridoxal phosphate binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}}
| Process = {{GNF_GO|id=GO:0006625 |text = protein targeting to peroxisome}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0046487 |text = glyoxylate metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 189
| Hs_Ensembl = ENSG00000172482
| Hs_RefseqProtein = NP_000021
| Hs_RefseqmRNA = NM_000030
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 241456835
| Hs_GenLoc_end = 241467210
| Hs_Uniprot = P21549
| Mm_EntrezGene = 11611
| Mm_Ensembl = ENSMUSG00000026272
| Mm_RefseqmRNA = XM_981336
| Mm_RefseqProtein = XP_986430
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 94965651
| Mm_GenLoc_end = 94975813
| Mm_Uniprot = Q3UEN9
}}
}}
'''Alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)''', also known as '''AGXT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=189| 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 is expressed only in the liver and the encoded protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targetting, have been associated with type I primary hyperoxaluria.<ref name="entrez">{{cite web | title = Entrez Gene: AGXT alanine-glyoxylate aminotransferase (oxalosis I; hyperoxaluria I; glycolicaciduria; serine-pyruvate aminotransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=189| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Danpure CJ |title=Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. |journal=Biochimie |volume=75 |issue= 3-4 |pages= 309-15 |year= 1993 |pmid= 8507692 |doi= }}
*{{cite journal | author=Danpure CJ |title=Molecular etiology of primary hyperoxaluria type 1: new directions for treatment. |journal=Am. J. Nephrol. |volume=25 |issue= 3 |pages= 303-10 |year= 2005 |pmid= 15961951 |doi= 10.1159/000086362 }}
*{{cite journal | author=Minatogawa Y, Tone S, Allsop J, ''et al.'' |title=A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. |journal=Hum. Mol. Genet. |volume=1 |issue= 8 |pages= 643-4 |year= 1993 |pmid= 1301173 |doi= }}
*{{cite journal | author=Purdue PE, Lumb MJ, Allsop J, ''et al.'' |title=A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. |journal=Genomics |volume=13 |issue= 1 |pages= 215-8 |year= 1992 |pmid= 1349575 |doi= }}
*{{cite journal | author=Purdue PE, Takada Y, Danpure CJ |title=Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. |journal=J. Cell Biol. |volume=111 |issue= 6 Pt 1 |pages= 2341-51 |year= 1991 |pmid= 1703535 |doi= }}
*{{cite journal | author=Purdue PE, Allsop J, Isaya G, ''et al.'' |title=Mistargeting of peroxisomal L-alanine:glyoxylate aminotransferase to mitochondria in primary hyperoxaluria patients depends upon activation of a cryptic mitochondrial targeting sequence by a point mutation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 23 |pages= 10900-4 |year= 1992 |pmid= 1961759 |doi= }}
*{{cite journal | author=Nishiyama K, Funai T, Katafuchi R, ''et al.'' |title=Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 3 |pages= 1093-9 |year= 1991 |pmid= 2039493 |doi= }}
*{{cite journal | author=Purdue PE, Lumb MJ, Fox M, ''et al.'' |title=Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. |journal=Genomics |volume=10 |issue= 1 |pages= 34-42 |year= 1991 |pmid= 2045108 |doi= }}
*{{cite journal | author=Nishiyama K, Berstein G, Oda T, Ichiyama A |title=Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. |journal=Eur. J. Biochem. |volume=194 |issue= 1 |pages= 9-18 |year= 1991 |pmid= 2253628 |doi= }}
*{{cite journal | author=Takada Y, Kaneko N, Esumi H, ''et al.'' |title=Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. |journal=Biochem. J. |volume=268 |issue= 2 |pages= 517-20 |year= 1990 |pmid= 2363689 |doi= }}
*{{cite journal | author=Danpure CJ, Jennings PR |title=Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I. |journal=FEBS Lett. |volume=201 |issue= 1 |pages= 20-4 |year= 1986 |pmid= 3709805 |doi= }}
*{{cite journal | author=Danpure CJ, Fryer P, Jennings PR, ''et al.'' |title=Evolution of alanine:glyoxylate aminotransferase 1 peroxisomal and mitochondrial targeting. A survey of its subcellular distribution in the livers of various representatives of the classes Mammalia, Aves and Amphibia. |journal=Eur. J. Cell Biol. |volume=64 |issue= 2 |pages= 295-313 |year= 1995 |pmid= 7813517 |doi= }}
*{{cite journal | author=Danpure CJ, Purdue PE, Fryer P, ''et al.'' |title=Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. |journal=Am. J. Hum. Genet. |volume=53 |issue= 2 |pages= 417-32 |year= 1993 |pmid= 8101040 |doi= }}
*{{cite journal | author=Minatogawa Y, Kawai C, Hatada S, Sato M |title=Liver specific kynurenine(alanine):glyoxylate aminotransferase was expressed in kidney cell line. |journal=Adv. Exp. Med. Biol. |volume=398 |issue= |pages= 471-6 |year= 1997 |pmid= 8906307 |doi= }}
*{{cite journal | author=von Schnakenburg C, Rumsby G |title=Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. |journal=J. Med. Genet. |volume=34 |issue= 6 |pages= 489-92 |year= 1997 |pmid= 9192270 |doi= }}
*{{cite journal | author=Amoroso A, Pirulli D, Puzzer D, ''et al.'' |title=Gene symbol: AGXT. Disease: primary hyperoxaluria type I. |journal=Hum. Genet. |volume=104 |issue= 5 |pages= 441 |year= 1999 |pmid= 10394939 |doi= }}
*{{cite journal | author=Pirulli D, Puzzer D, Ferri L, ''et al.'' |title=Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene. |journal=Hum. Genet. |volume=104 |issue= 6 |pages= 523-5 |year= 1999 |pmid= 10453743 |doi= }}
*{{cite journal | author=Basmaison O, Rolland MO, Cochat P, Bozon D |title=Identification of 5 novel mutations in the AGXT gene. |journal=Hum. Mutat. |volume=15 |issue= 6 |pages= 577 |year= 2000 |pmid= 10862087 |doi= 10.1002/1098-1004(200006)15:6<577::AID-HUMU9>3.0.CO;2-# }}
*{{cite journal | author=Lumb MJ, Danpure CJ |title=Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36415-22 |year= 2000 |pmid= 10960483 |doi= 10.1074/jbc.M006693200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ALDOB... {November 20, 2007 11:02:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:02:56 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ALDOB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fdj.
| PDB = {{PDB2|1fdj}}, {{PDB2|1qo5}}, {{PDB2|1xdl}}, {{PDB2|1xdm}}
| Name = Aldolase B, fructose-bisphosphate
| HGNCid = 417
| Symbol = ALDOB
| AltSymbols =;
| OMIM = 229600
| ECnumber =
| Homologene = 20060
| MGIid = 87995
| GeneAtlas_image1 = PBB_GE_ALDOB_211357_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ALDOB_204704_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ALDOB_204705_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004332 |text = fructose-bisphosphate aldolase activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006000 |text = fructose metabolic process}} {{GNF_GO|id=GO:0006096 |text = glycolysis}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 229
| Hs_Ensembl = ENSG00000136872
| Hs_RefseqProtein = NP_000026
| Hs_RefseqmRNA = NM_000035
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 103222681
| Hs_GenLoc_end = 103237926
| Hs_Uniprot = P05062
| Mm_EntrezGene = 230163
| Mm_Ensembl = ENSMUSG00000028307
| Mm_RefseqmRNA = NM_144903
| Mm_RefseqProtein = NP_659152
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 49557095
| Mm_GenLoc_end = 49570583
| Mm_Uniprot = Q3TJ66
}}
}}
'''Aldolase B, fructose-bisphosphate''', also known as '''ALDOB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ALDOB aldolase B, fructose-bisphosphate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=229| 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 = Fructose-1,6-bisphosphate aldolase (EC 4.1.2.13 ) is a tetrameric glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Vertebrates have 3 aldolase isozymes which are distinguished by their electrophoretic and catalytic properties. Differences indicate that aldolases A, B, and C are distinct proteins, the products of a family of related 'housekeeping' genes exhibiting developmentally regulated expression of the different isozymes. The developing embryo produces aldolase A, which is produced in even greater amounts in adult muscle where it can be as much as 5% of total cellular protein. In adult liver, kidney and intestine, aldolase A expression is repressed and aldolase B is produced. In brain and other nervous tissue, aldolase A and C are expressed about equally. There is a high degree of homology between aldolase A and C. Defects in ALDOB cause hereditary fructose intolerance.<ref name="entrez">{{cite web | title = Entrez Gene: ALDOB aldolase B, fructose-bisphosphate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=229| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tolan DR |title=Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene. |journal=Hum. Mutat. |volume=6 |issue= 3 |pages= 210-8 |year= 1996 |pmid= 8535439 |doi= 10.1002/humu.1380060303 }}
*{{cite journal | author=Cross NC, de Franchis R, Sebastio G, ''et al.'' |title=Molecular analysis of aldolase B genes in hereditary fructose intolerance. |journal=Lancet |volume=335 |issue= 8685 |pages= 306-9 |year= 1990 |pmid= 1967768 |doi= }}
*{{cite journal | author=Cross NC, Stojanov LM, Cox TM |title=A new aldolase B variant, N334K, is a common cause of hereditary fructose intolerance in Yugoslavia. |journal=Nucleic Acids Res. |volume=18 |issue= 7 |pages= 1925 |year= 1990 |pmid= 2336380 |doi= }}
*{{cite journal | author=Sakakibara M, Mukai T, Yatsuki H, Hori K |title=Human aldolase isozyme gene: the structure of multispecies aldolase B mRNAs. |journal=Nucleic Acids Res. |volume=13 |issue= 14 |pages= 5055-69 |year= 1985 |pmid= 2410860 |doi= }}
*{{cite journal | author=Sakakibara M, Takahashi I, Takasaki Y, ''et al.'' |title=Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host. |journal=Biochim. Biophys. Acta |volume=1007 |issue= 3 |pages= 334-42 |year= 1989 |pmid= 2649152 |doi= }}
*{{cite journal | author=Mukai T, Yatsuki H, Arai Y, ''et al.'' |title=Human aldolase B gene: characterization of the genomic aldolase B gene and analysis of sequences required for multiple polyadenylations. |journal=J. Biochem. |volume=102 |issue= 5 |pages= 1043-51 |year= 1988 |pmid= 2830249 |doi= }}
*{{cite journal | author=Henry I, Gallano P, Besmond C, ''et al.'' |title=The structural gene for aldolase B (ALDB) maps to 9q13----32. |journal=Ann. Hum. Genet. |volume=49 |issue= Pt 3 |pages= 173-80 |year= 1986 |pmid= 3000275 |doi= }}
*{{cite journal | author=Tolan DR, Penhoet EE |title=Characterization of the human aldolase B gene. |journal=Mol. Biol. Med. |volume=3 |issue= 3 |pages= 245-64 |year= 1986 |pmid= 3016456 |doi= }}
*{{cite journal | author=Cross NC, Tolan DR, Cox TM |title=Catalytic deficiency of human aldolase B in hereditary fructose intolerance caused by a common missense mutation. |journal=Cell |volume=53 |issue= 6 |pages= 881-5 |year= 1988 |pmid= 3383242 |doi= }}
*{{cite journal | author=Paolella G, Santamaria R, Izzo P, ''et al.'' |title=Isolation and nucleotide sequence of a full-length cDNA coding for aldolase B from human liver. |journal=Nucleic Acids Res. |volume=12 |issue= 19 |pages= 7401-10 |year= 1984 |pmid= 6548561 |doi= }}
*{{cite journal | author=Rottmann WH, Tolan DR, Penhoet EE |title=Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 9 |pages= 2738-42 |year= 1984 |pmid= 6585824 |doi= }}
*{{cite journal | author=Besmond C, Dreyfus JC, Gregori C, ''et al.'' |title=Nucleotide sequence of a cDNA clone for human aldolase B. |journal=Biochem. Biophys. Res. Commun. |volume=117 |issue= 2 |pages= 601-9 |year= 1984 |pmid= 6689266 |doi= }}
*{{cite journal | author=Ali M, Cox TM |title=Diverse mutations in the aldolase B gene that underlie the prevalence of hereditary fructose intolerance. |journal=Am. J. Hum. Genet. |volume=56 |issue= 4 |pages= 1002-5 |year= 1995 |pmid= 7717389 |doi= }}
*{{cite journal | author=Ali M, Sebastio G, Cox TM |title=Identification of a novel mutation (Leu 256-->Pro) in the human aldolase B gene associated with hereditary fructose intolerance. |journal=Hum. Mol. Genet. |volume=3 |issue= 1 |pages= 203-4 |year= 1994 |pmid= 8162030 |doi= }}
*{{cite journal | author=Brooks CC, Tolan DR |title=A partially active mutant aldolase B from a patient with hereditary fructose intolerance. |journal=FASEB J. |volume=8 |issue= 1 |pages= 107-13 |year= 1994 |pmid= 8299883 |doi= }}
*{{cite journal | author=Kusakabe T, Motoki K, Hori K |title=Mode of interactions of human aldolase isozymes with cytoskeletons. |journal=Arch. Biochem. Biophys. |volume=344 |issue= 1 |pages= 184-93 |year= 1997 |pmid= 9244396 |doi= 10.1006/abbi.1997.0204 }}
*{{cite journal | author=Lau J, Tolan DR |title=Screening for hereditary fructose intolerance mutations by reverse dot-blot. |journal=Mol. Cell. Probes |volume=13 |issue= 1 |pages= 35-40 |year= 1999 |pmid= 10024431 |doi= 10.1006/mcpr.1998.0208 }}
*{{cite journal | author=Santamaria R, Esposito G, Vitagliano L, ''et al.'' |title=Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase. |journal=Biochem. J. |volume=350 Pt 3 |issue= |pages= 823-8 |year= 2001 |pmid= 10970798 |doi= }}
*{{cite journal | author=Susan PP, Dunn WA |title=Starvation-induced lysosomal degradation of aldolase B requires glutamine 111 in a signal sequence for chaperone-mediated transport. |journal=J. Cell. Physiol. |volume=187 |issue= 1 |pages= 48-58 |year= 2001 |pmid= 11241348 |doi= 10.1002/1097-4652(2001)9999:9999<00::AID-JCP1050>3.0.CO;2-I }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AMY1A... {November 20, 2007 11:02:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:03:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_AMY1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b2y.
| PDB = {{PDB2|1b2y}}, {{PDB2|1bsi}}, {{PDB2|1c8q}}, {{PDB2|1cpu}}, {{PDB2|1hny}}, {{PDB2|1jxj}}, {{PDB2|1jxk}}, {{PDB2|1kb3}}, {{PDB2|1kbb}}, {{PDB2|1kbk}}, {{PDB2|1kgu}}, {{PDB2|1kgw}}, {{PDB2|1kgx}}, {{PDB2|1mfu}}, {{PDB2|1mfv}}, {{PDB2|1nm9}}, {{PDB2|1q4n}}, {{PDB2|1smd}}, {{PDB2|1u2y}}, {{PDB2|1u30}}, {{PDB2|1u33}}, {{PDB2|1xcw}}, {{PDB2|1xcx}}, {{PDB2|1xd0}}, {{PDB2|1xd1}}, {{PDB2|1xgz}}, {{PDB2|1xh0}}, {{PDB2|1xh1}}, {{PDB2|1xh2}}, {{PDB2|1xv8}}, {{PDB2|1z32}}, {{PDB2|2cpu}}, {{PDB2|3cpu}}
| Name = Amylase, alpha 1A; salivary
| HGNCid = 474
| Symbol = AMY1A
| AltSymbols =; AMY1; AMY1B
| OMIM = 104700
| ECnumber =
| Homologene = 86951
| MGIid = 88020
| Function = {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004556 |text = alpha-amylase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0031404 |text = chloride ion binding}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 276
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001127960
| Hs_RefseqmRNA = XM_001127960
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 11723
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009669
| Mm_RefseqProtein = NP_033799
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Amylase, alpha 1A; salivary''', also known as '''AMY1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMY1A amylase, alpha 1A; salivary| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=276| 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 = Amylases are secreted proteins that hydrolyze 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. The human genome has a cluster of several amylase genes that are expressed at high levels in either salivary gland or pancreas. This gene encodes an amylase isoenzyme produced by the salivary gland. Alternative splicing results in multiple transcript variants encoding the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: AMY1A amylase, alpha 1A; salivary| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=276| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bank RA, Hettema EH, Arwert F, ''et al.'' |title=Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase. |journal=Electrophoresis |volume=12 |issue= 1 |pages= 74-9 |year= 1991 |pmid= 1710976 |doi= 10.1002/elps.1150120114 }}
*{{cite journal | author=Groot PC, Mager WH, Henriquez NV, ''et al.'' |title=Evolution of the human alpha-amylase multigene family through unequal, homologous, and inter- and intrachromosomal crossovers. |journal=Genomics |volume=8 |issue= 1 |pages= 97-105 |year= 1991 |pmid= 2081604 |doi= }}
*{{cite journal | author=Nishide T, Nakamura Y, Emi M, ''et al.'' |title=Primary structure of human salivary alpha-amylase gene. |journal=Gene |volume=41 |issue= 2-3 |pages= 299-304 |year= 1986 |pmid= 2423416 |doi= }}
*{{cite journal | author=Davis MM, Hodes ME, Munsick RA, ''et al.'' |title=Pancreatic amylase expression in human pancreatic development. |journal=Hybridoma |volume=5 |issue= 2 |pages= 137-45 |year= 1986 |pmid= 2424823 |doi= }}
*{{cite journal | author=Handy DE, Larsen SH, Karn RC, Hodes ME |title=Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1. |journal=Mol. Biol. Med. |volume=4 |issue= 3 |pages= 145-55 |year= 1987 |pmid= 2442579 |doi= }}
*{{cite journal | author=Horii A, Emi M, Tomita N, ''et al.'' |title=Primary structure of human pancreatic alpha-amylase gene: its comparison with human salivary alpha-amylase gene. |journal=Gene |volume=60 |issue= 1 |pages= 57-64 |year= 1988 |pmid= 2450054 |doi= }}
*{{cite journal | author=Gumucio DL, Wiebauer K, Caldwell RM, ''et al.'' |title=Concerted evolution of human amylase genes. |journal=Mol. Cell. Biol. |volume=8 |issue= 3 |pages= 1197-205 |year= 1988 |pmid= 2452973 |doi= }}
*{{cite journal | author=Samuelson LC, Wiebauer K, Gumucio DL, Meisler MH |title=Expression of the human amylase genes: recent origin of a salivary amylase promoter from an actin pseudogene. |journal=Nucleic Acids Res. |volume=16 |issue= 17 |pages= 8261-76 |year= 1988 |pmid= 2458567 |doi= }}
*{{cite journal | author=Groot PC, Bleeker MJ, Pronk JC, ''et al.'' |title=The human alpha-amylase multigene family consists of haplotypes with variable numbers of genes. |journal=Genomics |volume=5 |issue= 1 |pages= 29-42 |year= 1989 |pmid= 2788608 |doi= }}
*{{cite journal | author=Pronk JC, Frants RR, Jansen W, ''et al.'' |title=Evidence of duplication of the human salivary amylase gene. |journal=Hum. Genet. |volume=60 |issue= 1 |pages= 32-5 |year= 1982 |pmid= 6176528 |doi= }}
*{{cite journal | author=Zabel BU, Naylor SL, Sakaguchi AY, ''et al.'' |title=High-resolution chromosomal localization of human genes for amylase, proopiomelanocortin, somatostatin, and a DNA fragment (D3S1) by in situ hybridization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 22 |pages= 6932-6 |year= 1984 |pmid= 6196780 |doi= }}
*{{cite journal | author=Tricoli JV, Shows TB |title=Regional assignment of human amylase (AMY) to p22----p21 of chromosome 1. |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 2 |pages= 205-10 |year= 1984 |pmid= 6608795 |doi= }}
*{{cite journal | author=Nishide T, Emi M, Nakamura Y, Matsubara K |title=Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] |journal=Gene |volume=28 |issue= 2 |pages= 263-70 |year= 1984 |pmid= 6610603 |doi= }}
*{{cite journal | author=Seyama K, Nukiwa T, Takahashi K, ''et al.'' |title=Amylase mRNA transcripts in normal tissues and neoplasms: the implication of different expressions of amylase isogenes. |journal=J. Cancer Res. Clin. Oncol. |volume=120 |issue= 4 |pages= 213-20 |year= 1994 |pmid= 7507116 |doi= }}
*{{cite journal | author=Ragunath C, Sundar K, Ramasubbu N |title=Expression, characterization, and biochemical properties of recombinant human salivary amylase. |journal=Protein Expr. Purif. |volume=24 |issue= 2 |pages= 202-11 |year= 2002 |pmid= 11858714 |doi= 10.1006/prep.2001.1559 }}
*{{cite journal | author=Hokari S, Miura K, Koyama I, ''et al.'' |title=A restriction endonuclease assay for expression of human alpha-amylase isozymes. |journal=Clin. Chim. Acta |volume=322 |issue= 1-2 |pages= 113-6 |year= 2002 |pmid= 12104089 |doi= }}
*{{cite journal | author=Furusawa M, Taira T, Iguchi-Ariga SM, Ariga H |title=AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, respectively, and inhibits cAMP-dependent protein kinase activity by preventing binding of its catalytic subunit to A-kinase-anchoring protein (AKAP) complex. |journal=J. Biol. Chem. |volume=277 |issue= 52 |pages= 50885-92 |year= 2003 |pmid= 12414807 |doi= 10.1074/jbc.M206387200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Ramasubbu N, Ragunath C, Mishra PJ |title=Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. |journal=J. Mol. Biol. |volume=325 |issue= 5 |pages= 1061-76 |year= 2003 |pmid= 12527308 |doi= }}
*{{cite journal | author=Kandra L, Gyémánt G, Remenyik J, ''et al.'' |title=Subsite mapping of human salivary alpha-amylase and the mutant Y151M. |journal=FEBS Lett. |volume=544 |issue= 1-3 |pages= 194-8 |year= 2003 |pmid= 12782315 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on APOD... {November 20, 2007 11:03:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:03:39 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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 = Apolipoprotein D
| HGNCid = 612
| Symbol = APOD
| AltSymbols =;
| OMIM = 107740
| ECnumber =
| Homologene = 1246
| MGIid = 88056
| GeneAtlas_image1 = PBB_GE_APOD_201525_at_tn.png
| Function = {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0005501 |text = retinoid binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008035 |text = high-density lipoprotein binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 347
| Hs_Ensembl = ENSG00000189058
| Hs_RefseqProtein = NP_001638
| Hs_RefseqmRNA = NM_001647
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 196776867
| Hs_GenLoc_end = 196792278
| Hs_Uniprot = P05090
| Mm_EntrezGene = 11815
| Mm_Ensembl = ENSMUSG00000022548
| Mm_RefseqmRNA = XM_994687
| Mm_RefseqProtein = XP_999781
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 31215939
| Mm_GenLoc_end = 31234343
| Mm_Uniprot = Q3TZE7
}}
}}
'''Apolipoprotein D''', also known as '''APOD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APOD apolipoprotein D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=347| 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 = Apolipoprotein D (Apo-D) is a component of high density lipoprotein that has no marked similarity to other apolipoprotein sequences. It has a high degree of homology to plasma retinol-binding protein and other members of the alpha 2 microglobulin protein superfamily of carrier proteins, also known as lipocalins. It is a glycoprotein of estimated molecular weight 33 KDa. Apo-D is closely associated with the enzyme lecithin:cholesterol acyltransferase - an enzyme involved in lipoprotein metabolism.<ref name="entrez">{{cite web | title = Entrez Gene: APOD apolipoprotein D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=347| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rassart E, Bedirian A, Do Carmo S, ''et al.'' |title=Apolipoprotein D. |journal=Biochim. Biophys. Acta |volume=1482 |issue= 1-2 |pages= 185-98 |year= 2000 |pmid= 11058760 |doi= }}
*{{cite journal | author=Peitsch MC, Boguski MS |title=Is apolipoprotein D a mammalian bilin-binding protein? |journal=New Biol. |volume=2 |issue= 2 |pages= 197-206 |year= 1991 |pmid= 2083249 |doi= }}
*{{cite journal | author=Balbín M, Freije JM, Fueyo A, ''et al.'' |title=Apolipoprotein D is the major protein component in cyst fluid from women with human breast gross cystic disease. |journal=Biochem. J. |volume=271 |issue= 3 |pages= 803-7 |year= 1990 |pmid= 2244881 |doi= }}
*{{cite journal | author=Drayna DT, McLean JW, Wion KL, ''et al.'' |title=Human apolipoprotein D gene: gene sequence, chromosome localization, and homology to the alpha 2u-globulin superfamily. |journal=DNA |volume=6 |issue= 3 |pages= 199-204 |year= 1987 |pmid= 2439269 |doi= }}
*{{cite journal | author=Drayna D, Scott JD, Lawn R |title=Multiple RFLPs at the human apolipoprotein D (APOD) locus. |journal=Nucleic Acids Res. |volume=15 |issue= 22 |pages= 9617 |year= 1988 |pmid= 2891117 |doi= }}
*{{cite journal | author=Drayna D, Fielding C, McLean J, ''et al.'' |title=Cloning and expression of human apolipoprotein D cDNA. |journal=J. Biol. Chem. |volume=261 |issue= 35 |pages= 16535-9 |year= 1987 |pmid= 3453108 |doi= }}
*{{cite journal | author=Fielding PE, Fielding CJ |title=A cholesteryl ester transfer complex in human plasma. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=77 |issue= 6 |pages= 3327-30 |year= 1980 |pmid= 6774335 |doi= }}
*{{cite journal | author=Schindler PA, Settineri CA, Collet X, ''et al.'' |title=Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion. |journal=Protein Sci. |volume=4 |issue= 4 |pages= 791-803 |year= 1995 |pmid= 7613477 |doi= }}
*{{cite journal | author=Yang CY, Gu ZW, Blanco-Vaca F, ''et al.'' |title=Structure of human apolipoprotein D: locations of the intermolecular and intramolecular disulfide links. |journal=Biochemistry |volume=33 |issue= 41 |pages= 12451-5 |year= 1994 |pmid= 7918467 |doi= }}
*{{cite journal | author=Holzfeind P, Merschak P, Dieplinger H, Redl B |title=The human lacrimal gland synthesizes apolipoprotein D mRNA in addition to tear prealbumin mRNA, both species encoding members of the lipocalin superfamily. |journal=Exp. Eye Res. |volume=61 |issue= 4 |pages= 495-500 |year= 1996 |pmid= 8549691 |doi= }}
*{{cite journal | author=Zeng C, Spielman AI, Vowels BR, ''et al.'' |title=A human axillary odorant is carried by apolipoprotein D. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6626-30 |year= 1996 |pmid= 8692868 |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=Liu Z, Chang GQ, Leibowitz SF |title=Apolipoprotein D interacts with the long-form leptin receptor: a hypothalamic function in the control of energy homeostasis. |journal=FASEB J. |volume=15 |issue= 7 |pages= 1329-31 |year= 2001 |pmid= 11344130 |doi= }}
*{{cite journal | author=Sánchez D, Ganfornina MD, Martínez S |title=Expression pattern of the lipocalin apolipoprotein D during mouse embryogenesis. |journal=Mech. Dev. |volume=110 |issue= 1-2 |pages= 225-9 |year= 2002 |pmid= 11744388 |doi= }}
*{{cite journal | author=Mahadik SP, Khan MM, Evans DR, Parikh VV |title=Elevated plasma level of apolipoprotein D in schizophrenia and its treatment and outcome. |journal=Schizophr. Res. |volume=58 |issue= 1 |pages= 55-62 |year= 2002 |pmid= 12363390 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Desai PP, Hendrie HC, Evans RM, ''et al.'' |title=Genetic variation in apolipoprotein D affects the risk of Alzheimer disease in African-Americans. |journal=Am. J. Med. Genet. B Neuropsychiatr. Genet. |volume=116 |issue= 1 |pages= 98-101 |year= 2003 |pmid= 12497622 |doi= 10.1002/ajmg.b.10798 }}
*{{cite journal | author=Kang MK, Kameta A, Shin KH, ''et al.'' |title=Senescence-associated genes in normal human oral keratinocytes. |journal=Exp. Cell Res. |volume=287 |issue= 2 |pages= 272-81 |year= 2003 |pmid= 12837283 |doi= }}
*{{cite journal | author=Thomas EA, Laws SM, Sutcliffe JG, ''et al.'' |title=Apolipoprotein D levels are elevated in prefrontal cortex of subjects with Alzheimer's disease: no relation to apolipoprotein E expression or genotype. |journal=Biol. Psychiatry |volume=54 |issue= 2 |pages= 136-41 |year= 2003 |pmid= 12873803 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on B4GALT1... {November 20, 2007 11:08:07 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein B4GALT1 image.jpg {November 20, 2007 11:08:46 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:09:09 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_B4GALT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nf5.
| PDB = {{PDB2|1nf5}}, {{PDB2|1nhe}}, {{PDB2|1nkh}}, {{PDB2|1nmm}}, {{PDB2|1nqi}}, {{PDB2|1nwg}}, {{PDB2|1o0r}}, {{PDB2|1o23}}, {{PDB2|1oqm}}, {{PDB2|2ae7}}, {{PDB2|2aec}}, {{PDB2|2aes}}, {{PDB2|2agd}}, {{PDB2|2ah9}}, {{PDB2|2fy7}}, {{PDB2|2fya}}, {{PDB2|2fyb}}
| Name = UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1
| HGNCid = 924
| Symbol = B4GALT1
| AltSymbols =; GTB; B4GAL-T1; DKFZp686N19253; GGTB2; GT1; MGC50983; beta4Gal-T1
| OMIM = 137060
| ECnumber =
| Homologene = 20378
| MGIid = 95705
| GeneAtlas_image1 = PBB_GE_B4GALT1_201883_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_B4GALT1_201882_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_B4GALT1_211631_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003831 |text = beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity}} {{GNF_GO|id=GO:0003945 |text = N-acetyllactosamine synthase activity}} {{GNF_GO|id=GO:0004461 |text = lactose synthase activity}} {{GNF_GO|id=GO:0008378 |text = galactosyltransferase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006012 |text = galactose metabolic process}} {{GNF_GO|id=GO:0009312 |text = oligosaccharide biosynthetic process}} {{GNF_GO|id=GO:0030198 |text = extracellular matrix organization and biogenesis}} {{GNF_GO|id=GO:0045136 |text = development of secondary sexual characteristics}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2683
| Hs_Ensembl = ENSG00000086062
| Hs_RefseqProtein = NP_001488
| Hs_RefseqmRNA = NM_001497
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 33100635
| Hs_GenLoc_end = 33157354
| Hs_Uniprot = P15291
| Mm_EntrezGene = 14595
| Mm_Ensembl = ENSMUSG00000028413
| Mm_RefseqmRNA = NM_022305
| Mm_RefseqProtein = NP_071641
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 40993273
| Mm_GenLoc_end = 41042669
| Mm_Uniprot = Q05CE5
}}
}}
'''UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1''', also known as '''B4GALT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: B4GALT1 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2683| 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 is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene is unique among the beta4GalT genes because it encodes an enzyme that participates both in glycoconjugate and lactose biosynthesis. For the first activity, the enzyme adds galactose to N-acetylglucosamine residues that are either monosaccharides or the nonreducing ends of glycoprotein carbohydrate chains. The second activity is restricted to lactating mammary tissues where the enzyme forms a heterodimer with alpha-lactalbumin to catalyze UDP-galactose + D-glucose <=> UDP + lactose. The two enzymatic forms result from alternate transcription initiation sites and post-translational processing. Two transcripts, which differ only at the 5' end, with approximate lengths of 4.1 kb and 3.9 kb encode the same protein. The longer transcript encodes the type II membrane-bound, trans-Golgi resident protein involved in glycoconjugate biosynthesis. The shorter transcript encodes a protein which is cleaved to form the soluble lactose synthase.<ref name="entrez">{{cite web | title = Entrez Gene: B4GALT1 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2683| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Amado M, Almeida R, Schwientek T, Clausen H |title=Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. |journal=Biochim. Biophys. Acta |volume=1473 |issue= 1 |pages= 35-53 |year= 2000 |pmid= 10580128 |doi= }}
*{{cite journal | author=Gerber AC, Kozdrowski I, Wyss SR, Berger EG |title=The charge heterogeneity of soluble human galactosyltransferases isolated from milk, amniotic fluid and malignant ascites. |journal=Eur. J. Biochem. |volume=93 |issue= 3 |pages= 453-60 |year= 1979 |pmid= 33805 |doi= }}
*{{cite journal | author=Uejima T, Uemura M, Nozawa S, Narimatsu H |title=Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies. |journal=Cancer Res. |volume=52 |issue= 22 |pages= 6158-63 |year= 1992 |pmid= 1384956 |doi= }}
*{{cite journal | author=Lopez LC, Youakim A, Evans SC, Shur BD |title=Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase. |journal=J. Biol. Chem. |volume=266 |issue= 24 |pages= 15984-91 |year= 1991 |pmid= 1714903 |doi= }}
*{{cite journal | author=Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC |title=Genomic structure and expression of human beta-1,4-galactosyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 3 |pages= 1269-76 |year= 1991 |pmid= 1903938 |doi= }}
*{{cite journal | author=Aoki D, Appert HE, Johnson D, ''et al.'' |title=Analysis of the substrate binding sites of human galactosyltransferase by protein engineering. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3171-8 |year= 1990 |pmid= 2120039 |doi= }}
*{{cite journal | author=Watzele G, Berger EG |title=Near identity of HeLa cell galactosyltransferase with the human placental enzyme. |journal=Nucleic Acids Res. |volume=18 |issue= 23 |pages= 7174 |year= 1991 |pmid= 2124683 |doi= }}
*{{cite journal | author=Kalyanaraman VS, Rodriguez V, Veronese F, ''et al.'' |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371-80 |year= 1990 |pmid= 2187500 |doi= }}
*{{cite journal | author=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384-8 |year= 1989 |pmid= 2541446 |doi= }}
*{{cite journal | author=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452-6 |year= 1989 |pmid= 2542563 |doi= }}
*{{cite journal | author=Kozarsky K, Penman M, Basiripour L, ''et al.'' |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163-9 |year= 1989 |pmid= 2649653 |doi= }}
*{{cite journal | author=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265-82 |year= 1988 |pmid= 2829950 |doi= }}
*{{cite journal | author=Appert HE, Rutherford TJ, Tarr GE, ''et al.'' |title=Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence. |journal=Biochem. Biophys. Res. Commun. |volume=138 |issue= 1 |pages= 224-9 |year= 1986 |pmid= 3091013 |doi= }}
*{{cite journal | author=Appert HE, Rutherford TJ, Tarr GE, ''et al.'' |title=Isolation of a cDNA coding for human galactosyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=139 |issue= 1 |pages= 163-8 |year= 1986 |pmid= 3094506 |doi= }}
*{{cite journal | author=Furukawa K, Roth S, Sawicki J |title=Several galactosyltransferase activities are associated with mouse chromosome 17. |journal=Genetics |volume=114 |issue= 3 |pages= 983-91 |year= 1987 |pmid= 3098628 |doi= }}
*{{cite journal | author=Masri KA, Appert HE, Fukuda MN |title=Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase). |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 2 |pages= 657-63 |year= 1989 |pmid= 3144273 |doi= }}
*{{cite journal | author=Roth J, Lentze MJ, Berger EG |title=Immunocytochemical demonstration of ecto-galactosyltransferase in absorptive intestinal cells. |journal=J. Cell Biol. |volume=100 |issue= 1 |pages= 118-25 |year= 1985 |pmid= 3917437 |doi= }}
*{{cite journal | author=Roth J, Berger EG |title=Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae. |journal=J. Cell Biol. |volume=93 |issue= 1 |pages= 223-9 |year= 1982 |pmid= 6121819 |doi= }}
*{{cite journal | author=Chatterjee SK, Mukerjee S, Tripathi PK |title=Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones. |journal=Int. J. Biochem. Cell Biol. |volume=27 |issue= 3 |pages= 329-36 |year= 1995 |pmid= 7540104 |doi= }}
*{{cite journal | author=Kudo T, Narimatsu H |title=The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells. |journal=Glycobiology |volume=5 |issue= 4 |pages= 397-403 |year= 1995 |pmid= 7579794 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COL6A2... {November 20, 2007 11:03:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:04:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
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| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Collagen, type VI, alpha 2
| HGNCid = 2212
| Symbol = COL6A2
| AltSymbols =; DKFZp586E1322; PP3610
| OMIM = 120240
| ECnumber =
| Homologene = 1392
| MGIid = 88460
| GeneAtlas_image1 = PBB_GE_COL6A2_209156_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_COL6A2_213290_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0030198 |text = extracellular matrix organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1292
| Hs_Ensembl = ENSG00000142173
| Hs_RefseqProtein = NP_001840
| Hs_RefseqmRNA = NM_001849
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 46342470
| Hs_GenLoc_end = 46377189
| Hs_Uniprot = P12110
| Mm_EntrezGene = 12834
| Mm_Ensembl = ENSMUSG00000020241
| Mm_RefseqmRNA = XM_973905
| Mm_RefseqProtein = XP_978999
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 76039478
| Mm_GenLoc_end = 76067043
| Mm_Uniprot = Q8C972
}}
}}
'''Collagen, type VI, alpha 2''', also known as '''COL6A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COL6A2 collagen, type VI, alpha 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1292| 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 one of the three alpha chains of type VI collagen, a beaded filament collagen found in most connective tissues. The product of this gene contains several domains similar to von Willebrand Factor type A domains. These domains have been shown to bind extracellular matrix proteins, an interaction that explains the importance of this collagen in organizing matrix components. Mutations in this gene are associated with Bethlem myopathy and Ullrich scleroatonic muscular dystrophy. Three transcript variants have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: COL6A2 collagen, type VI, alpha 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1292| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bertini E, Pepe G |title=Collagen type VI and related disorders: Bethlem myopathy and Ullrich scleroatonic muscular dystrophy. |journal=Eur. J. Paediatr. Neurol. |volume=6 |issue= 4 |pages= 193-8 |year= 2002 |pmid= 12374585 |doi= }}
*{{cite journal | author=Lampe AK, Bushby KM |title=Collagen VI related muscle disorders. |journal=J. Med. Genet. |volume=42 |issue= 9 |pages= 673-85 |year= 2006 |pmid= 16141002 |doi= 10.1136/jmg.2002.002311 }}
*{{cite journal | author=Bidanset DJ, Guidry C, Rosenberg LC, ''et al.'' |title=Binding of the proteoglycan decorin to collagen type VI. |journal=J. Biol. Chem. |volume=267 |issue= 8 |pages= 5250-6 |year= 1992 |pmid= 1544908 |doi= }}
*{{cite journal | author=Saitta B, Timpl R, Chu ML |title=Human alpha 2(VI) collagen gene. Heterogeneity at the 5'-untranslated region generated by an alternate exon. |journal=J. Biol. Chem. |volume=267 |issue= 9 |pages= 6188-96 |year= 1992 |pmid= 1556127 |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=Saitta B, Stokes DG, Vissing H, ''et al.'' |title=Alternative splicing of the human alpha 2(VI) collagen gene generates multiple mRNA transcripts which predict three protein variants with distinct carboxyl termini. |journal=J. Biol. Chem. |volume=265 |issue= 11 |pages= 6473-80 |year= 1990 |pmid= 1690728 |doi= }}
*{{cite journal | author=Saitta B, Wang YM, Renkart L, ''et al.'' |title=The exon organization of the triple-helical coding regions of the human alpha 1(VI) and alpha 2(VI) collagen genes is highly similar. |journal=Genomics |volume=11 |issue= 1 |pages= 145-53 |year= 1992 |pmid= 1765372 |doi= }}
*{{cite journal | author=Chu ML, Pan TC, Conway D, ''et al.'' |title=Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of human type VI collagen reveals internal triplication of globular domains similar to the A domains of von Willebrand factor and two alpha 2(VI) chain variants that differ in the carboxy terminus. |journal=EMBO J. |volume=8 |issue= 7 |pages= 1939-46 |year= 1989 |pmid= 2551668 |doi= }}
*{{cite journal | author=Chu ML, Conway D, Pan TC, ''et al.'' |title=Amino acid sequence of the triple-helical domain of human collagen type VI. |journal=J. Biol. Chem. |volume=263 |issue= 35 |pages= 18601-6 |year= 1989 |pmid= 3198591 |doi= }}
*{{cite journal | author=Weil D, Mattei MG, Passage E, ''et al.'' |title=Cloning and chromosomal localization of human genes encoding the three chains of type VI collagen. |journal=Am. J. Hum. Genet. |volume=42 |issue= 3 |pages= 435-45 |year= 1988 |pmid= 3348212 |doi= }}
*{{cite journal | author=Chu ML, Mann K, Deutzmann R, ''et al.'' |title=Characterization of three constituent chains of collagen type VI by peptide sequences and cDNA clones. |journal=Eur. J. Biochem. |volume=168 |issue= 2 |pages= 309-17 |year= 1987 |pmid= 3665927 |doi= }}
*{{cite journal | author=Jander R, Rauterberg J, Glanville RW |title=Further characterization of the three polypeptide chains of bovine and human short-chain collagen (intima collagen). |journal=Eur. J. Biochem. |volume=133 |issue= 1 |pages= 39-46 |year= 1983 |pmid= 6852033 |doi= }}
*{{cite journal | author=Tillet E, Wiedemann H, Golbik R, ''et al.'' |title=Recombinant expression and structural and binding properties of alpha 1(VI) and alpha 2(VI) chains of human collagen type VI. |journal=Eur. J. Biochem. |volume=221 |issue= 1 |pages= 177-85 |year= 1994 |pmid= 8168508 |doi= }}
*{{cite journal | author=Nishiyama A, Stallcup WB |title=Expression of NG2 proteoglycan causes retention of type VI collagen on the cell surface. |journal=Mol. Biol. Cell |volume=4 |issue= 11 |pages= 1097-108 |year= 1994 |pmid= 8305732 |doi= }}
*{{cite journal | author=Jöbsis GJ, Keizers H, Vreijling JP, ''et al.'' |title=Type VI collagen mutations in Bethlem myopathy, an autosomal dominant myopathy with contractures. |journal=Nat. Genet. |volume=14 |issue= 1 |pages= 113-5 |year= 1996 |pmid= 8782832 |doi= 10.1038/ng0996-113 }}
*{{cite journal | author=Tillet E, Ruggiero F, Nishiyama A, Stallcup WB |title=The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein. |journal=J. Biol. Chem. |volume=272 |issue= 16 |pages= 10769-76 |year= 1997 |pmid= 9099729 |doi= }}
*{{cite journal | author=Kuo HJ, Maslen CL, Keene DR, Glanville RW |title=Type VI collagen anchors endothelial basement membranes by interacting with type IV collagen. |journal=J. Biol. Chem. |volume=272 |issue= 42 |pages= 26522-9 |year= 1997 |pmid= 9334230 |doi= }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=Camacho Vanegas O, Bertini E, Zhang RZ, ''et al.'' |title=Ullrich scleroatonic muscular dystrophy is caused by recessive mutations in collagen type VI. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 13 |pages= 7516-21 |year= 2001 |pmid= 11381124 |doi= 10.1073/pnas.121027598 }}
*{{cite journal | author=Scacheri PC, Gillanders EM, Subramony SH, ''et al.'' |title=Novel mutations in collagen VI genes: expansion of the Bethlem myopathy phenotype. |journal=Neurology |volume=58 |issue= 4 |pages= 593-602 |year= 2002 |pmid= 11865138 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CPE... {November 20, 2007 11:04:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:04:29 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 =
| image_source =
| PDB =
| Name = Carboxypeptidase E
| HGNCid = 2303
| Symbol = CPE
| AltSymbols =;
| OMIM = 114855
| ECnumber =
| Homologene = 48052
| MGIid = 101932
| GeneAtlas_image1 = PBB_GE_CPE_201117_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CPE_201116_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004180 |text = carboxypeptidase activity}} {{GNF_GO|id=GO:0004182 |text = carboxypeptidase A activity}} {{GNF_GO|id=GO:0004183 |text = carboxypeptidase E activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007218 |text = neuropeptide signaling pathway}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0030070 |text = insulin processing}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1363
| Hs_Ensembl = ENSG00000109472
| Hs_RefseqProtein = NP_001864
| Hs_RefseqmRNA = NM_001873
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 166519824
| Hs_GenLoc_end = 166638908
| Hs_Uniprot = P16870
| Mm_EntrezGene = 12876
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_976304
| Mm_RefseqProtein = XP_981398
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Carboxypeptidase E''', also known as '''CPE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CPE carboxypeptidase E| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1363| 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 = Carboxypeptidase E cleaves C-terminal amino acid residues and is involved in neuropeptide processing. It is a peripheral membrane protein. CPE specifically binds regulated secretory pathway proteins, including prohormones, but not constitutively secreted proteins.<ref name="entrez">{{cite web | title = Entrez Gene: CPE carboxypeptidase E| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1363| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Goodge KA, Hutton JC |title=Translational regulation of proinsulin biosynthesis and proinsulin conversion in the pancreatic beta-cell. |journal=Semin. Cell Dev. Biol. |volume=11 |issue= 4 |pages= 235-42 |year= 2000 |pmid= 10966857 |doi= 10.1006/scdb.2000.0172 }}
*{{cite journal | author=Beinfeld MC |title=Biosynthesis and processing of pro CCK: recent progress and future challenges. |journal=Life Sci. |volume=72 |issue= 7 |pages= 747-57 |year= 2003 |pmid= 12479974 |doi= }}
*{{cite journal | author=Manser E, Fernandez D, Loo L, ''et al.'' |title=Human carboxypeptidase E. Isolation and characterization of the cDNA, sequence conservation, expression and processing in vitro. |journal=Biochem. J. |volume=267 |issue= 2 |pages= 517-25 |year= 1990 |pmid= 2334405 |doi= }}
*{{cite journal | author=Fricker LD, Snyder SH |title=Enkephalin convertase: purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=79 |issue= 12 |pages= 3886-90 |year= 1982 |pmid= 6808517 |doi= }}
*{{cite journal | author=O'Rahilly S, Gray H, Humphreys PJ, ''et al.'' |title=Brief report: impaired processing of prohormones associated with abnormalities of glucose homeostasis and adrenal function. |journal=N. Engl. J. Med. |volume=333 |issue= 21 |pages= 1386-90 |year= 1995 |pmid= 7477119 |doi= }}
*{{cite journal | author=Naggert JK, Fricker LD, Varlamov O, ''et al.'' |title=Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity. |journal=Nat. Genet. |volume=10 |issue= 2 |pages= 135-42 |year= 1995 |pmid= 7663508 |doi= 10.1038/ng0695-135 }}
*{{cite journal | author=Song L, Fricker L |title=Processing of procarboxypeptidase E into carboxypeptidase E occurs in secretory vesicles. |journal=J. Neurochem. |volume=65 |issue= 1 |pages= 444-53 |year= 1995 |pmid= 7790890 |doi= }}
*{{cite journal | author=Hall C, Manser E, Spurr NK, Lim L |title=Assignment of the human carboxypeptidase E (CPE) gene to chromosome 4. |journal=Genomics |volume=15 |issue= 2 |pages= 461-3 |year= 1993 |pmid= 8449522 |doi= 10.1006/geno.1993.1093 }}
*{{cite journal | author=Guest PC, Arden SD, Rutherford NG, Hutton JC |title=The post-translational processing and intracellular sorting of carboxypeptidase H in the islets of Langerhans. |journal=Mol. Cell. Endocrinol. |volume=113 |issue= 1 |pages= 99-108 |year= 1996 |pmid= 8674818 |doi= }}
*{{cite journal | author=Rovere C, Viale A, Nahon J, Kitabgi P |title=Impaired processing of brain proneurotensin and promelanin-concentrating hormone in obese fat/fat mice. |journal=Endocrinology |volume=137 |issue= 7 |pages= 2954-8 |year= 1996 |pmid= 8770919 |doi= }}
*{{cite journal | author=Alcalde L, Tonacchera M, Costagliola S, ''et al.'' |title=Cloning of candidate autoantigen carboxypeptidase H from a human islet library: sequence identity with human brain CPH. |journal=J. Autoimmun. |volume=9 |issue= 4 |pages= 525-8 |year= 1996 |pmid= 8864828 |doi= 10.1006/jaut.1996.0070 }}
*{{cite journal | author=Cool DR, Normant E, Shen F, ''et al.'' |title=Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpe(fat) mice. |journal=Cell |volume=88 |issue= 1 |pages= 73-83 |year= 1997 |pmid= 9019408 |doi= }}
*{{cite journal | author=Maeda K, Okubo K, Shimomura I, ''et al.'' |title=Analysis of an expression profile of genes in the human adipose tissue. |journal=Gene |volume=190 |issue= 2 |pages= 227-35 |year= 1997 |pmid= 9197538 |doi= }}
*{{cite journal | author=Cain BM, Wang W, Beinfeld MC |title=Cholecystokinin (CCK) levels are greatly reduced in the brains but not the duodenums of Cpe(fat)/Cpe(fat) mice: a regional difference in the involvement of carboxypeptidase E (Cpe) in pro-CCK processing. |journal=Endocrinology |volume=138 |issue= 9 |pages= 4034-7 |year= 1997 |pmid= 9275097 |doi= }}
*{{cite journal | author=Lacourse KA, Friis-Hansen L, Rehfeld JF, Samuelson LC |title=Disturbed progastrin processing in carboxypeptidase E-deficient fat mice. |journal=FEBS Lett. |volume=416 |issue= 1 |pages= 45-50 |year= 1997 |pmid= 9369230 |doi= }}
*{{cite journal | author=Utsunomiya N, Ohagi S, Sanke T, ''et al.'' |title=Organization of the human carboxypeptidase E gene and molecular scanning for mutations in Japanese subjects with NIDDM or obesity. |journal=Diabetologia |volume=41 |issue= 6 |pages= 701-5 |year= 1998 |pmid= 9662053 |doi= }}
*{{cite journal | author=Reznik SE, Salafia CM, Lage JM, Fricker LD |title=Immunohistochemical localization of carboxypeptidases E and D in the human placenta and umbilical cord. |journal=J. Histochem. Cytochem. |volume=46 |issue= 12 |pages= 1359-68 |year= 1999 |pmid= 9815277 |doi= }}
*{{cite journal | author=Fan X, Olson SJ, Johnson MD |title=Immunohistochemical localization and comparison of carboxypeptidases D, E, and Z, alpha-MSH, ACTH, and MIB-1 between human anterior and corticotroph cell "basophil invasion" of the posterior pituitary. |journal=J. Histochem. Cytochem. |volume=49 |issue= 6 |pages= 783-90 |year= 2001 |pmid= 11373325 |doi= }}
*{{cite journal | author=Friis-Hansen L, Lacourse KA, Samuelson LC, Holst JJ |title=Attenuated processing of proglucagon and glucagon-like peptide-1 in carboxypeptidase E-deficient mice. |journal=J. Endocrinol. |volume=169 |issue= 3 |pages= 595-602 |year= 2001 |pmid= 11375130 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CPOX... {November 20, 2007 11:04:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:04:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CPOX_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2aex.
| PDB = {{PDB2|2aex}}
| Name = Coproporphyrinogen oxidase
| HGNCid = 2321
| Symbol = CPOX
| AltSymbols =; HCP; CPO; CPX
| OMIM = 121300
| ECnumber =
| Homologene = 76
| MGIid = 104841
| GeneAtlas_image1 = PBB_GE_CPOX_204172_at_tn.png
| Function = {{GNF_GO|id=GO:0004109 |text = coproporphyrinogen oxidase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006783 |text = heme biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1371
| Hs_Ensembl = ENSG00000080819
| Hs_RefseqProtein = NP_000088
| Hs_RefseqmRNA = NM_000097
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 99780982
| Hs_GenLoc_end = 99795131
| Hs_Uniprot = P36551
| Mm_EntrezGene = 12892
| Mm_Ensembl = ENSMUSG00000022742
| Mm_RefseqmRNA = NM_007757
| Mm_RefseqProtein = NP_031783
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 58612835
| Mm_GenLoc_end = 58622904
| Mm_Uniprot = Q3U029
}}
}}
'''Coproporphyrinogen oxidase''', also known as '''CPOX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CPOX coproporphyrinogen oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1371| 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=Lamoril J, Martasek P, Deybach JC, ''et al.'' |title=A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria. |journal=Hum. Mol. Genet. |volume=4 |issue= 2 |pages= 275-8 |year= 1995 |pmid= 7757079 |doi= }}
*{{cite journal | author=Fujita H, Kondo M, Taketani S, ''et al.'' |title=Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria. |journal=Hum. Mol. Genet. |volume=3 |issue= 10 |pages= 1807-10 |year= 1995 |pmid= 7849704 |doi= }}
*{{cite journal | author=Cacheux V, Martasek P, Fougerousse F, ''et al.'' |title=Localization of the human coproporphyrinogen oxidase gene to chromosome band 3q12. |journal=Hum. Genet. |volume=94 |issue= 5 |pages= 557-9 |year= 1994 |pmid= 7959694 |doi= }}
*{{cite journal | author=Delfau-Larue MH, Martasek P, Grandchamp B |title=Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping. |journal=Hum. Mol. Genet. |volume=3 |issue= 8 |pages= 1325-30 |year= 1995 |pmid= 7987309 |doi= }}
*{{cite journal | author=Martasek P, Nordmann Y, Grandchamp B |title=Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms. |journal=Hum. Mol. Genet. |volume=3 |issue= 3 |pages= 477-80 |year= 1994 |pmid= 8012360 |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=Martasek P, Camadro JM, Delfau-Larue MH, ''et al.'' |title=Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 3024-8 |year= 1994 |pmid= 8159699 |doi= }}
*{{cite journal | author=Taketani S, Kohno H, Furukawa T, ''et al.'' |title=Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase. |journal=Biochim. Biophys. Acta |volume=1183 |issue= 3 |pages= 547-9 |year= 1994 |pmid= 8286403 |doi= }}
*{{cite journal | author=Kohno H, Furukawa T, Yoshinaga T, ''et al.'' |title=Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation. |journal=J. Biol. Chem. |volume=268 |issue= 28 |pages= 21359-63 |year= 1993 |pmid= 8407975 |doi= }}
*{{cite journal | author=Lamoril J, Deybach JC, Puy H, ''et al.'' |title=Three novel mutations in the coproporphyrinogen oxidase gene. |journal=Hum. Mutat. |volume=9 |issue= 1 |pages= 78-80 |year= 1997 |pmid= 8990017 |doi= 10.1002/(SICI)1098-1004(1997)9:1<78::AID-HUMU17>3.0.CO;2-M }}
*{{cite journal | author=Daimon M, Gojyou E, Sugawara M, ''et al.'' |title=A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria. |journal=Hum. Genet. |volume=99 |issue= 2 |pages= 199-201 |year= 1997 |pmid= 9048920 |doi= }}
*{{cite journal | author=Schreiber WE, Zhang X, Senz J, Jamani A |title=Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene. |journal=Hum. Mutat. |volume=10 |issue= 3 |pages= 196-200 |year= 1997 |pmid= 9298818 |doi= 10.1002/(SICI)1098-1004(1997)10:3<196::AID-HUMU3>3.0.CO;2-H }}
*{{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=Lamoril J, Puy H, Gouya L, ''et al.'' |title=Neonatal hemolytic anemia due to inherited harderoporphyria: clinical characteristics and molecular basis. |journal=Blood |volume=91 |issue= 4 |pages= 1453-7 |year= 1998 |pmid= 9454777 |doi= }}
*{{cite journal | author=Susa S, Daimon M, Kondo H, ''et al.'' |title=Identification of a novel mutation of the CPO gene in a Japanese hereditary coproporphyria family. |journal=Am. J. Med. Genet. |volume=80 |issue= 3 |pages= 204-6 |year= 1999 |pmid= 9843038 |doi= }}
*{{cite journal | author=Rosipal R, Lamoril J, Puy H, ''et al.'' |title=Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update. |journal=Hum. Mutat. |volume=13 |issue= 1 |pages= 44-53 |year= 1999 |pmid= 9888388 |doi= 10.1002/(SICI)1098-1004(1999)13:1<44::AID-HUMU5>3.0.CO;2-Q }}
*{{cite journal | author=Taketani S, Furukawa T, Furuyama K |title=Expression of coproporphyrinogen oxidase and synthesis of hemoglobin in human erythroleukemia K562 cells. |journal=Eur. J. Biochem. |volume=268 |issue= 6 |pages= 1705-11 |year= 2001 |pmid= 11248690 |doi= }}
*{{cite journal | author=Lamoril J, Puy H, Whatley SD, ''et al.'' |title=Characterization of mutations in the CPO gene in British patients demonstrates absence of genotype-phenotype correlation and identifies relationship between hereditary coproporphyria and harderoporphyria. |journal=Am. J. Hum. Genet. |volume=68 |issue= 5 |pages= 1130-8 |year= 2001 |pmid= 11309681 |doi= }}
*{{cite journal | author=Elkon H, Don J, Melamed E, ''et al.'' |title=Mutant and wild-type alpha-synuclein interact with mitochondrial cytochrome C oxidase. |journal=J. Mol. Neurosci. |volume=18 |issue= 3 |pages= 229-38 |year= 2003 |pmid= 12059041 |doi= }}
*{{cite journal | author=Wiman A, Floderus Y, Harper P |title=Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria. |journal=J. Hum. Genet. |volume=47 |issue= 8 |pages= 407-12 |year= 2002 |pmid= 12181641 |doi= 10.1007/s100380200059 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DCK... {November 20, 2007 11:04:52 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:05:21 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DCK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p5z.
| PDB = {{PDB2|1p5z}}, {{PDB2|1p60}}, {{PDB2|1p61}}, {{PDB2|1p62}}, {{PDB2|2a2z}}, {{PDB2|2a30}}, {{PDB2|2a7q}}, {{PDB2|2no9}}, {{PDB2|2noa}}
| Name = Deoxycytidine kinase
| HGNCid = 2704
| Symbol = DCK
| AltSymbols =; MGC117410; MGC138632
| OMIM = 125450
| ECnumber =
| Homologene = 616
| MGIid = 102726
| GeneAtlas_image1 = PBB_GE_DCK_203302_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004137 |text = deoxycytidine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016773 |text = phosphotransferase activity, alcohol group as acceptor}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006139 |text = nucleobase, nucleoside, nucleotide and nucleic acid metabolic process}} {{GNF_GO|id=GO:0006220 |text = pyrimidine nucleotide metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1633
| Hs_Ensembl = ENSG00000156136
| Hs_RefseqProtein = NP_000779
| Hs_RefseqmRNA = NM_000788
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 72078256
| Hs_GenLoc_end = 72115477
| Hs_Uniprot = P27707
| Mm_EntrezGene = 13178
| Mm_Ensembl = ENSMUSG00000029366
| Mm_RefseqmRNA = XM_977104
| Mm_RefseqProtein = XP_982198
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 89839588
| Mm_GenLoc_end = 89857838
| Mm_Uniprot = Q545E8
}}
}}
'''Deoxycytidine kinase''', also known as '''DCK''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DCK deoxycytidine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1633| 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 = Deoxycytidine kinase (DCK) is required for the phosphorylation of several deoxyribonucleosides and their nucleoside analogs. Deficiency of DCK is associated with resistance to antiviral and anticancer chemotherapeutic agents. Conversely, increased deoxycytidine kinase activity is associated with increased activation of these compounds to cytotoxic nucleoside triphosphate derivatives. DCK is clinically important because of its relationship to drug resistance and sensitivity.<ref name="entrez">{{cite web | title = Entrez Gene: DCK deoxycytidine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1633| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Arnér ES, Eriksson S |title=Mammalian deoxyribonucleoside kinases. |journal=Pharmacol. Ther. |volume=67 |issue= 2 |pages= 155-86 |year= 1996 |pmid= 7494863 |doi= }}
*{{cite journal | author=Chottiner EG, Shewach DS, Datta NS, ''et al.'' |title=Cloning and expression of human deoxycytidine kinase cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 4 |pages= 1531-5 |year= 1991 |pmid= 1996353 |doi= }}
*{{cite journal | author=Eriksson S, Cederlund E, Bergman T, ''et al.'' |title=Characterization of human deoxycytidine kinase. Correlation with cDNA sequences. |journal=FEBS Lett. |volume=280 |issue= 2 |pages= 363-6 |year= 1991 |pmid= 2013338 |doi= }}
*{{cite journal | author=Yamada Y, Goto H, Ogasawara N |title=Purine nucleoside kinases in human T- and B-lymphoblasts. |journal=Biochim. Biophys. Acta |volume=761 |issue= 1 |pages= 34-40 |year= 1984 |pmid= 6315069 |doi= }}
*{{cite journal | author=Hurley MC, Palella TD, Fox IH |title=Human placental deoxyadenosine and deoxyguanosine phosphorylating activity. |journal=J. Biol. Chem. |volume=258 |issue= 24 |pages= 15021-7 |year= 1984 |pmid= 6317685 |doi= }}
*{{cite journal | author=Spasokoukotskaja T, Arnér ES, Brosjö O, ''et al.'' |title=Expression of deoxycytidine kinase and phosphorylation of 2-chlorodeoxyadenosine in human normal and tumour cells and tissues. |journal=Eur. J. Cancer |volume=31A |issue= 2 |pages= 202-8 |year= 1995 |pmid= 7718326 |doi= }}
*{{cite journal | author=Stegmann AP, Honders MW, Bolk MW, ''et al.'' |title=Assignment of the human deoxycytidine kinase (DCK) gene to chromosome 4 band q13.3-q21.1. |journal=Genomics |volume=17 |issue= 2 |pages= 528-9 |year= 1993 |pmid= 8406512 |doi= 10.1006/geno.1993.1365 }}
*{{cite journal | author=Song JJ, Walker S, Chen E, ''et al.'' |title=Genomic structure and chromosomal localization of the human deoxycytidine kinase gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 2 |pages= 431-4 |year= 1993 |pmid= 8421671 |doi= }}
*{{cite journal | author=Johansson M, Brismar S, Karlsson A |title=Human deoxycytidine kinase is located in the cell nucleus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 22 |pages= 11941-5 |year= 1997 |pmid= 9342341 |doi= }}
*{{cite journal | author=Hatzis P, Al-Madhoon AS, Jüllig M, ''et al.'' |title=The intracellular localization of deoxycytidine kinase. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30239-43 |year= 1998 |pmid= 9804782 |doi= }}
*{{cite journal | author=Saada A, Shaag A, Mandel H, ''et al.'' |title=Mutant mitochondrial thymidine kinase in mitochondrial DNA depletion myopathy. |journal=Nat. Genet. |volume=29 |issue= 3 |pages= 342-4 |year= 2001 |pmid= 11687801 |doi= 10.1038/ng751 }}
*{{cite journal | author=Veuger MJ, Heemskerk MH, Honders MW, ''et al.'' |title=Functional role of alternatively spliced deoxycytidine kinase in sensitivity to cytarabine of acute myeloid leukemic cells. |journal=Blood |volume=99 |issue= 4 |pages= 1373-80 |year= 2002 |pmid= 11830489 |doi= }}
*{{cite journal | author=Innoceta A, Galluzzi L, Ruzzo A, ''et al.'' |title=Molecular basis of 2',3'-dideoxycytidine-induced drug resistance in human cells. |journal=Mol. Cell. Biochem. |volume=231 |issue= 1-2 |pages= 173-7 |year= 2002 |pmid= 11952160 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Krawiec K, Kierdaszuk B, Shugar D |title=Inorganic tripolyphosphate (PPP(i)) as a phosphate donor for human deoxyribonucleoside kinases. |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 1 |pages= 192-7 |year= 2003 |pmid= 12535661 |doi= }}
*{{cite journal | author=van der Wilt CL, Kroep JR, Loves WJ, ''et al.'' |title=Expression of deoxycytidine kinase in leukaemic cells compared with solid tumour cell lines, liver metastases and normal liver. |journal=Eur. J. Cancer |volume=39 |issue= 5 |pages= 691-7 |year= 2003 |pmid= 12628850 |doi= }}
*{{cite journal | author=Ge Y, Jensen TL, Matherly LH, Taub JW |title=Physical and functional interactions between USF and Sp1 proteins regulate human deoxycytidine kinase promoter activity. |journal=J. Biol. Chem. |volume=278 |issue= 50 |pages= 49901-10 |year= 2004 |pmid= 14514691 |doi= 10.1074/jbc.M305085200 }}
*{{cite journal | author=Usova E, Maltseva T, Földesi A, ''et al.'' |title=Human deoxycytidine kinase as a deoxyribonucleoside phosphorylase. |journal=J. Mol. Biol. |volume=344 |issue= 5 |pages= 1347-58 |year= 2005 |pmid= 15561147 |doi= 10.1016/j.jmb.2004.10.016 }}
*{{cite journal | author=Mani RS, Usova EV, Eriksson S, Cass CE |title=Fluorescence studies of substrate binding to human recombinant deoxycytidine kinase. |journal=Nucleosides Nucleotides Nucleic Acids |volume=23 |issue= 8-9 |pages= 1343-6 |year= 2005 |pmid= 15571255 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DNASE1... {November 20, 2007 11:05:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:06:02 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Deoxyribonuclease I
| HGNCid = 2956
| Symbol = DNASE1
| AltSymbols =; DNL1; DRNI; FLJ38093
| OMIM = 125505
| ECnumber =
| Homologene = 3826
| MGIid = 103157
| GeneAtlas_image1 = PBB_GE_DNASE1_210165_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004530 |text = deoxyribonuclease I activity}} {{GNF_GO|id=GO:0004536 |text = deoxyribonuclease activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006308 |text = DNA catabolic process}} {{GNF_GO|id=GO:0006915 |text = apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1773
| Hs_Ensembl = ENSG00000126594
| Hs_RefseqProtein = NP_005214
| Hs_RefseqmRNA = NM_005223
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 3630847
| Hs_GenLoc_end = 3654064
| Hs_Uniprot = P24855
| Mm_EntrezGene = 13419
| Mm_Ensembl = ENSMUSG00000005980
| Mm_RefseqmRNA = NM_010061
| Mm_RefseqProtein = NP_034191
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 3952371
| Mm_GenLoc_end = 3955247
| Mm_Uniprot = Q14BW6
}}
}}
'''Deoxyribonuclease I''', also known as '''DNASE1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DNASE1 deoxyribonuclease I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1773| 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 DNase family. This protein is stored in the zymogen granules of the nuclear envelope and functions by cleaving DNA in an endonucleolytic manner. At least six autosomal codominant alleles have been characterized, DNASE1*1 through DNASE1*6, and the sequence of DNASE1*2 represented in this record. Mutations in this gene have been associated with systemic lupus erythematosus (SLE), an autoimmune disease. A recombinant form of this protein is used to treat the one of the symptoms of cystic fibrosis by hydrolyzing the extracellular DNA in sputum and reducing its viscosity. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.<ref name="entrez">{{cite web | title = Entrez Gene: DNASE1 deoxyribonuclease I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1773| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lachmann PJ |title=Lupus and desoxyribonuclease. |journal=Lupus |volume=12 |issue= 3 |pages= 202-6 |year= 2003 |pmid= 12708782 |doi= }}
*{{cite journal | author=Shak S, Capon DJ, Hellmiss R, ''et al.'' |title=Recombinant human DNase I reduces the viscosity of cystic fibrosis sputum. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 23 |pages= 9188-92 |year= 1991 |pmid= 2251263 |doi= }}
*{{cite journal | author=Yasuda T, Awazu S, Sato W, ''et al.'' |title=Human genetically polymorphic deoxyribonuclease: purification, characterization, and multiplicity of urine deoxyribonuclease I. |journal=J. Biochem. |volume=108 |issue= 3 |pages= 393-8 |year= 1991 |pmid= 2277032 |doi= }}
*{{cite journal | author=Kishi K, Yasuda T, Ikehara Y, ''et al.'' |title=Human serum deoxyribonuclease I (DNase I) polymorphism: pattern similarities among isozymes from serum, urine, kidney, liver, and pancreas. |journal=Am. J. Hum. Genet. |volume=47 |issue= 1 |pages= 121-6 |year= 1990 |pmid= 2349940 |doi= }}
*{{cite journal | author=Kabsch W, Mannherz HG, Suck D, ''et al.'' |title=Atomic structure of the actin:DNase I complex. |journal=Nature |volume=347 |issue= 6288 |pages= 37-44 |year= 1990 |pmid= 2395459 |doi= 10.1038/347037a0 }}
*{{cite journal | author=Kishi K, Yasuda T, Awazu S, Mizuta K |title=Genetic polymorphism of human urine deoxyribonuclease I. |journal=Hum. Genet. |volume=81 |issue= 3 |pages= 295-7 |year= 1989 |pmid= 2921043 |doi= }}
*{{cite journal | author=Rosenstreich DL, Tu JH, Kinkade PR, ''et al.'' |title=A human urine-derived interleukin 1 inhibitor. Homology with deoxyribonuclease I. |journal=J. Exp. Med. |volume=168 |issue= 5 |pages= 1767-79 |year= 1988 |pmid= 3263467 |doi= }}
*{{cite journal | author=Yasuda T, Nadano D, Takeshita H, ''et al.'' |title=Molecular analysis of the third allele of human deoxyribonuclease I polymorphism. |journal=Ann. Hum. Genet. |volume=59 |issue= Pt 2 |pages= 139-47 |year= 1995 |pmid= 7625762 |doi= }}
*{{cite journal | author=Yasuda T, Kishi K, Yanagawa Y, Yoshida A |title=Structure of the human deoxyribonuclease I (DNase I) gene: identification of the nucleotide substitution that generates its classical genetic polymorphism. |journal=Ann. Hum. Genet. |volume=59 |issue= Pt 1 |pages= 1-15 |year= 1995 |pmid= 7762978 |doi= }}
*{{cite journal | author=Yasuda T, Nadano D, Iida R, ''et al.'' |title=Chromosomal assignment of the human deoxyribonuclease I gene, DNASE 1 (DNL1), to band 16p13.3 using the polymerase chain reaction. |journal=Cytogenet. Cell Genet. |volume=70 |issue= 3-4 |pages= 221-3 |year= 1995 |pmid= 7789176 |doi= }}
*{{cite journal | author=Yasuda T, Nadano D, Takeshita H, ''et al.'' |title=The molecular basis for genetic polymorphism of human deoxyribonuclease I: identification of the nucleotide substitution that generates the fourth allele. |journal=FEBS Lett. |volume=359 |issue= 2-3 |pages= 211-4 |year= 1995 |pmid= 7867802 |doi= }}
*{{cite journal | author=Yasuda T, Nadano D, Tenjo E, ''et al.'' |title=Genotyping of human deoxyribonuclease I polymorphism by the polymerase chain reaction. |journal=Electrophoresis |volume=16 |issue= 10 |pages= 1889-93 |year= 1996 |pmid= 8586059 |doi= }}
*{{cite journal | author=Iida R, Yasuda T, Takeshita H, ''et al.'' |title=Identification of the nucleotide substitution that generates the fourth polymorphic site in human deoxyribonuclease I (DNase I). |journal=Hum. Genet. |volume=98 |issue= 4 |pages= 415-8 |year= 1996 |pmid= 8792814 |doi= }}
*{{cite journal | author=Iida R, Yasuda T, Aoyama M, ''et al.'' |title=The fifth allele of the human deoxyribonuclease I (DNase I) polymorphism. |journal=Electrophoresis |volume=18 |issue= 11 |pages= 1936-9 |year= 1998 |pmid= 9420147 |doi= 10.1002/elps.1150181108 }}
*{{cite journal | author=Yasuda T, Takeshita H, Iida R, ''et al.'' |title=A new allele, DNASE1*6, of human deoxyribonuclease I polymorphism encodes an Arg to Cys substitution responsible for its instability. |journal=Biochem. Biophys. Res. Commun. |volume=260 |issue= 1 |pages= 280-3 |year= 1999 |pmid= 10381379 |doi= 10.1006/bbrc.1999.0900 }}
*{{cite journal | author=Oliveri M, Daga A, Cantoni C, ''et al.'' |title=DNase I mediates internucleosomal DNA degradation in human cells undergoing drug-induced apoptosis. |journal=Eur. J. Immunol. |volume=31 |issue= 3 |pages= 743-51 |year= 2001 |pmid= 11241278 |doi= }}
*{{cite journal | author=Otterbein LR, Graceffa P, Dominguez R |title=The crystal structure of uncomplexed actin in the ADP state. |journal=Science |volume=293 |issue= 5530 |pages= 708-11 |year= 2001 |pmid= 11474115 |doi= 10.1126/science.1059700 }}
*{{cite journal | author=Yasutomo K, Horiuchi T, Kagami S, ''et al.'' |title=Mutation of DNASE1 in people with systemic lupus erythematosus. |journal=Nat. Genet. |volume=28 |issue= 4 |pages= 313-4 |year= 2001 |pmid= 11479590 |doi= 10.1038/91070 }}
*{{cite journal | author=Ballweber E, Galla M, Aktories K, ''et al.'' |title=Interaction of ADP-ribosylated actin with actin binding proteins. |journal=FEBS Lett. |volume=508 |issue= 1 |pages= 131-5 |year= 2001 |pmid= 11707283 |doi= }}
*{{cite journal | author=Tsutsumi S, Kaneko Y, Asao T, ''et al.'' |title=DNase I is present in the chief cells of human and rat stomachs. |journal=Histochem. J. |volume=33 |issue= 9-10 |pages= 531-5 |year= 2002 |pmid= 12005024 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ENO2... {November 20, 2007 11:06:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:06:26 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ENO2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1te6.
| PDB = {{PDB2|1te6}}, {{PDB2|2akm}}, {{PDB2|2akz}}
| Name = Enolase 2 (gamma, neuronal)
| HGNCid = 3353
| Symbol = ENO2
| AltSymbols =; NSE
| OMIM = 131360
| ECnumber =
| Homologene = 74414
| MGIid = 95394
| GeneAtlas_image1 = PBB_GE_ENO2_201313_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004634 |text = phosphopyruvate hydratase activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}}
| Component = {{GNF_GO|id=GO:0000015 |text = phosphopyruvate hydratase complex}}
| Process = {{GNF_GO|id=GO:0006096 |text = glycolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2026
| Hs_Ensembl = ENSG00000111674
| Hs_RefseqProtein = NP_001966
| Hs_RefseqmRNA = NM_001975
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 6893875
| Hs_GenLoc_end = 6903120
| Hs_Uniprot = P09104
| Mm_EntrezGene = 13807
| Mm_Ensembl = ENSMUSG00000004267
| Mm_RefseqmRNA = NM_013509
| Mm_RefseqProtein = NP_038537
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 124725672
| Mm_GenLoc_end = 124735128
| Mm_Uniprot = Q3UJ20
}}
}}
'''Enolase 2 (gamma, neuronal)''', also known as '''ENO2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ENO2 enolase 2 (gamma, neuronal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2026| 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 one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in mature neurons and cells of neuronal origin. A switch from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.<ref name="entrez">{{cite web | title = Entrez Gene: ENO2 enolase 2 (gamma, neuronal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2026| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Oliva D, Calì L, Feo S, Giallongo A |title=Complete structure of the human gene encoding neuron-specific enolase. |journal=Genomics |volume=10 |issue= 1 |pages= 157-65 |year= 1991 |pmid= 2045099 |doi= }}
*{{cite journal | author=Craig SP, Day IN, Thompson RJ, Craig IW |title=Localisation of neurone-specific enolase (ENO2) to 12p13. |journal=Cytogenet. Cell Genet. |volume=54 |issue= 1-2 |pages= 71-3 |year= 1991 |pmid= 2249478 |doi= }}
*{{cite journal | author=Oliva D, Barba G, Barbieri G, ''et al.'' |title=Cloning, expression and sequence homologies of cDNA for human gamma enolase. |journal=Gene |volume=79 |issue= 2 |pages= 355-60 |year= 1989 |pmid= 2792767 |doi= }}
*{{cite journal | author=McAleese SM, Dunbar B, Fothergill JE, ''et al.'' |title=Complete amino acid sequence of the neurone-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE). |journal=Eur. J. Biochem. |volume=178 |issue= 2 |pages= 413-7 |year= 1989 |pmid= 3208766 |doi= }}
*{{cite journal | author=Van Obberghen E, Kamholz J, Bishop JG, ''et al.'' |title=Human gamma enolase: isolation of a cDNA clone and expression in normal and tumor tissues of human origin. |journal=J. Neurosci. Res. |volume=19 |issue= 4 |pages= 450-6 |year= 1988 |pmid= 3385803 |doi= 10.1002/jnr.490190409 }}
*{{cite journal | author=Day IN, Allsopp MT, Moore DC, Thompson RJ |title=Sequence conservation in the 3'-untranslated regions of neurone-specific enolase, lymphokine and protooncogene mRNAs. |journal=FEBS Lett. |volume=222 |issue= 1 |pages= 139-43 |year= 1987 |pmid= 3653393 |doi= }}
*{{cite journal | author=Haimoto H, Takahashi Y, Koshikawa T, ''et al.'' |title=Immunohistochemical localization of gamma-enolase in normal human tissues other than nervous and neuroendocrine tissues. |journal=Lab. Invest. |volume=52 |issue= 3 |pages= 257-63 |year= 1985 |pmid= 3974199 |doi= }}
*{{cite journal | author=Quan CP, Watanabe S, Vuillier F, ''et al.'' |title=Purification and partial amino acid sequence of suppressive lymphokine from a CD8+ CD57+ human T hybridoma. |journal=Immunology |volume=78 |issue= 2 |pages= 205-9 |year= 1993 |pmid= 7682534 |doi= }}
*{{cite journal | author=Angelov DN, Neiss WF, Gunkel A, ''et al.'' |title=Axotomy induces intranuclear immunolocalization of neuron-specific enolase in facial and hypoglossal neurons of the rat. |journal=J. Neurocytol. |volume=23 |issue= 4 |pages= 218-33 |year= 1994 |pmid= 8035205 |doi= }}
*{{cite journal | author=Pechumer H, Bender-Götze C, Ziegler-Heitbrock HW |title=Detection of neuron-specific gamma-enolase messenger ribonucleic acid in normal human leukocytes by polymerase chain reaction amplification with nested primers. |journal=Lab. Invest. |volume=69 |issue= 6 |pages= 743-9 |year= 1994 |pmid= 8264236 |doi= }}
*{{cite journal | author=Ansari-Lari MA, Shen Y, Muzny DM, ''et al.'' |title=Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. |journal=Genome Res. |volume=7 |issue= 3 |pages= 268-80 |year= 1997 |pmid= 9074930 |doi= }}
*{{cite journal | author=Lau L |title=Neuroblastoma: a single institution's experience with 128 children and an evaluation of clinical and biological prognostic factors. |journal=Pediatric hematology and oncology |volume=19 |issue= 2 |pages= 79-89 |year= 2002 |pmid= 11881792 |doi= }}
*{{cite journal | author=Wijnberger LD, Nikkels PG, van Dongen AJ, ''et al.'' |title=Expression in the placenta of neuronal markers for perinatal brain damage. |journal=Pediatr. Res. |volume=51 |issue= 4 |pages= 492-6 |year= 2002 |pmid= 11919335 |doi= }}
*{{cite journal | author=O'Dwyer DT, Clifton V, Hall A, ''et al.'' |title=Pituitary autoantibodies in lymphocytic hypophysitis target both gamma- and alpha-Enolase - a link with pregnancy? |journal=Arch. Physiol. Biochem. |volume=110 |issue= 1-2 |pages= 94-8 |year= 2002 |pmid= 11935405 |doi= }}
*{{cite journal | author=Chekhonin VP, Zhirkov YA, Belyaeva IA, ''et al.'' |title=Serum time course of two brain-specific proteins, alpha(1) brain globulin and neuron-specific enolase, in tick-born encephalitis and Lyme disease. |journal=Clin. Chim. Acta |volume=320 |issue= 1-2 |pages= 117-25 |year= 2002 |pmid= 11983209 |doi= }}
*{{cite journal | author=Nakatsuka S, Nishiu M, Tomita Y, ''et al.'' |title=Enhanced expression of neuron-specific enolase (NSE) in pyothorax-associated lymphoma (PAL). |journal=Jpn. J. Cancer Res. |volume=93 |issue= 4 |pages= 411-6 |year= 2005 |pmid= 11985791 |doi= }}
*{{cite journal | author=Fujiwara H, Arima N, Ohtsubo H, ''et al.'' |title=Clinical significance of serum neuron-specific enolase in patients with adult T-cell leukemia. |journal=Am. J. Hematol. |volume=71 |issue= 2 |pages= 80-4 |year= 2002 |pmid= 12353304 |doi= 10.1002/ajh.10190 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Rodríguez-Núñez A, Cid E, Rodríguez-García J, ''et al.'' |title=Neuron-specific enolase, nucleotides, nucleosides, purine bases, oxypurines and uric acid concentrations in cerebrospinal fluid of children with meningitis. |journal=Brain Dev. |volume=25 |issue= 2 |pages= 102-6 |year= 2003 |pmid= 12581805 |doi= }}
*{{cite journal | author=Muley T, Ebert W, Stieber P, ''et al.'' |title=Technical performance and diagnostic utility of the new Elecsys neuron-specific enolase enzyme immunoassay. |journal=Clin. Chem. Lab. Med. |volume=41 |issue= 1 |pages= 95-103 |year= 2003 |pmid= 12636057 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EPB41L3... {November 20, 2007 11:18:16 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein EPB41L3 image.jpg {November 20, 2007 11:19:30 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:19:53 PM PST}
- CREATED: Created new protein page: EPB41L3 {November 20, 2007 11:20:05 PM PST}
- INFO: Beginning work on EPB42... {November 20, 2007 11:06:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:06:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| update_summary = yes
| update_citations = yes
}}
<!-- 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 = Erythrocyte membrane protein band 4.2
| HGNCid = 3381
| Symbol = EPB42
| AltSymbols =; PA; MGC116735; MGC116737
| OMIM = 177070
| ECnumber =
| Homologene = 93
| MGIid = 95402
| GeneAtlas_image1 = PBB_GE_EPB42_210746_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005524 |text = ATP binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0008360 |text = regulation of cell shape}} {{GNF_GO|id=GO:0018149 |text = peptide cross-linking}} {{GNF_GO|id=GO:0043249 |text = erythrocyte maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2038
| Hs_Ensembl = ENSG00000166947
| Hs_RefseqProtein = NP_000110
| Hs_RefseqmRNA = NM_000119
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 41276720
| Hs_GenLoc_end = 41300773
| Hs_Uniprot = P16452
| Mm_EntrezGene = 13828
| Mm_Ensembl = ENSMUSG00000023216
| Mm_RefseqmRNA = NM_013513
| Mm_RefseqProtein = NP_038541
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 120709332
| Mm_GenLoc_end = 120728513
| Mm_Uniprot = Q3T9M7
}}
}}
'''Erythrocyte membrane protein band 4.2''', also known as '''EPB42''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPB42 erythrocyte membrane protein band 4.2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2038| 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 = Erythrocyte membrane protein band 4.2 is an ATP-binding protein which may regulate the association of protein 3 with ankyrin. It probably has a role in erythrocyte shape and mechanical property regulation. Mutations in the EPB42 gene are associated with recessive spherocytic elliptocytosis and recessively transmitted hereditary hemolytic anemia.<ref name="entrez">{{cite web | title = Entrez Gene: EPB42 erythrocyte membrane protein band 4.2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2038| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Falcón-Pérez JM, Dell'Angelica EC |title=The pallidin (Pldn) gene and the role of SNARE proteins in melanosome biogenesis. |journal=Pigment Cell Res. |volume=15 |issue= 2 |pages= 82-6 |year= 2002 |pmid= 11936273 |doi= }}
*{{cite journal | author=White RA, Peters LL, Adkison LR, ''et al.'' |title=The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene. |journal=Nat. Genet. |volume=2 |issue= 1 |pages= 80-3 |year= 1993 |pmid= 1284644 |doi= 10.1038/ng0992-80 }}
*{{cite journal | author=Sung LA, Chien S, Fan YS, ''et al.'' |title=Human erythrocyte protein 4.2: isoform expression, differential splicing, and chromosomal assignment. |journal=Blood |volume=79 |issue= 10 |pages= 2763-70 |year= 1992 |pmid= 1350227 |doi= }}
*{{cite journal | author=Risinger MA, Dotimas EM, Cohen CM |title=Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. |journal=J. Biol. Chem. |volume=267 |issue= 8 |pages= 5680-5 |year= 1992 |pmid= 1544941 |doi= }}
*{{cite journal | author=Bouhassira EE, Schwartz RS, Yawata Y, ''et al.'' |title=An alanine-to-threonine substitution in protein 4.2 cDNA is associated with a Japanese form of hereditary hemolytic anemia (protein 4.2NIPPON). |journal=Blood |volume=79 |issue= 7 |pages= 1846-54 |year= 1992 |pmid= 1558976 |doi= }}
*{{cite journal | author=Sung LA, Chien S, Chang LS, ''et al.'' |title=Molecular cloning of human protein 4.2: a major component of the erythrocyte membrane. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 3 |pages= 955-9 |year= 1990 |pmid= 1689063 |doi= }}
*{{cite journal | author=Najfeld V, Ballard SG, Menninger J, ''et al.'' |title=The gene for human erythrocyte protein 4.2 maps to chromosome 15q15. |journal=Am. J. Hum. Genet. |volume=50 |issue= 1 |pages= 71-5 |year= 1992 |pmid= 1729896 |doi= }}
*{{cite journal | author=Low PS, Willardson BM, Mohandas N, ''et al.'' |title=Contribution of the band 3-ankyrin interaction to erythrocyte membrane mechanical stability. |journal=Blood |volume=77 |issue= 7 |pages= 1581-6 |year= 1991 |pmid= 1826225 |doi= }}
*{{cite journal | author=Korsgren C, Cohen CM |title=Organization of the gene for human erythrocyte membrane protein 4.2: structural similarities with the gene for the a subunit of factor XIII. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 11 |pages= 4840-4 |year= 1991 |pmid= 2052563 |doi= }}
*{{cite journal | author=Korsgren C, Lawler J, Lambert S, ''et al.'' |title=Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 613-7 |year= 1990 |pmid= 2300550 |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=Tanimoto T, Hoshijima M, Kawata M, ''et al.'' |title=Binding of ras p21 to bands 4.2 and 6 of human erythrocyte membranes. |journal=FEBS Lett. |volume=226 |issue= 2 |pages= 291-6 |year= 1988 |pmid= 3276554 |doi= }}
*{{cite journal | author=Rybicki AC, Musto S, Schwartz RS |title=Identification of a band-3 binding site near the N-terminus of erythrocyte membrane protein 4.2. |journal=Biochem. J. |volume=309 ( Pt 2) |issue= |pages= 677-81 |year= 1995 |pmid= 7626035 |doi= }}
*{{cite journal | author=Hayette S, Morle L, Bozon M, ''et al.'' |title=A point mutation in the protein 4.2 gene (allele 4.2 Tozeur) associated with hereditary haemolytic anaemia. |journal=Br. J. Haematol. |volume=89 |issue= 4 |pages= 762-70 |year= 1995 |pmid= 7772513 |doi= }}
*{{cite journal | author=Hayette S, Dhermy D, dos Santos ME, ''et al.'' |title=A deletional frameshift mutation in protein 4.2 gene (allele 4.2 Lisboa) associated with hereditary hemolytic anemia. |journal=Blood |volume=85 |issue= 1 |pages= 250-6 |year= 1995 |pmid= 7803799 |doi= }}
*{{cite journal | author=Takaoka Y, Ideguchi H, Matsuda M, ''et al.'' |title=A novel mutation in the erythrocyte protein 4.2 gene of Japanese patients with hereditary spherocytosis (protein 4.2 Fukuoka). |journal=Br. J. Haematol. |volume=88 |issue= 3 |pages= 527-33 |year= 1995 |pmid= 7819064 |doi= }}
*{{cite journal | author=Das AK, Bhattacharya R, Kundu M, ''et al.'' |title=Human erythrocyte membrane protein 4.2 is palmitoylated. |journal=Eur. J. Biochem. |volume=224 |issue= 2 |pages= 575-80 |year= 1994 |pmid= 7925374 |doi= }}
*{{cite journal | author=Dotimas E, Speicher DW, GuptaRoy B, Cohen CM |title=Structural domain mapping and phosphorylation of human erythrocyte pallidin (band 4.2). |journal=Biochim. Biophys. Acta |volume=1148 |issue= 1 |pages= 19-29 |year= 1993 |pmid= 8499466 |doi= }}
*{{cite journal | author=Azim AC, Marfatia SM, Korsgren C, ''et al.'' |title=Human erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteins. |journal=Biochemistry |volume=35 |issue= 9 |pages= 3001-6 |year= 1996 |pmid= 8608138 |doi= 10.1021/bi951745y }}
*{{cite journal | author=Bhattacharyya R, Das AK, Moitra PK, ''et al.'' |title=Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2. |journal=Biochem. J. |volume=340 ( Pt 2) |issue= |pages= 505-12 |year= 1999 |pmid= 10333496 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FLT3LG... {November 20, 2007 11:06:55 PM PST}
- SEARCH REDIRECT: Control Box Found: FLT3LG {November 20, 2007 11:07:16 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 20, 2007 11:07:17 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 20, 2007 11:07:17 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 20, 2007 11:07:17 PM PST}
- UPDATED: Updated protein page: FLT3LG {November 20, 2007 11:07:22 PM PST}
- INFO: Beginning work on GCN5L2... {November 20, 2007 11:07:22 PM PST}
- SEARCH REDIRECT: Control Box Found: GCN5L2 {November 20, 2007 11:07:55 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 20, 2007 11:07:58 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 20, 2007 11:07:58 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 20, 2007 11:07:58 PM PST}
- UPDATED: Updated protein page: GCN5L2 {November 20, 2007 11:08:07 PM PST}
- INFO: Beginning work on HRH2... {November 20, 2007 11:10:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:10:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Histamine receptor H2
| HGNCid = 5183
| Symbol = HRH2
| AltSymbols =; H2R
| OMIM = 142703
| ECnumber =
| Homologene = 40613
| MGIid = 108482
| GeneAtlas_image1 = PBB_GE_HRH2_220805_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004969 |text = histamine receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3274
| Hs_Ensembl = ENSG00000113749
| Hs_RefseqProtein = NP_071640
| Hs_RefseqmRNA = NM_022304
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 175017637
| Hs_GenLoc_end = 175045847
| Hs_Uniprot = P25021
| Mm_EntrezGene = 15466
| Mm_Ensembl = ENSMUSG00000034987
| Mm_RefseqmRNA = NM_001010973
| Mm_RefseqProtein = NP_001010973
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 54201750
| Mm_GenLoc_end = 54232053
| Mm_Uniprot = Q3ZB30
}}
}}
'''Histamine receptor H2''', also known as '''HRH2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HRH2 histamine receptor H2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3274| 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 = Histamine is a ubiquitous messenger molecule released from mast cells, enterochromaffin-like cells, and neurons. Its various actions are mediated by histamine receptors H1, H2, H3 and H4. Histamine receptor H2 belongs to the family 1 of G protein-coupled receptors. It is an integral membrane protein and stimulates gastric acid secretion. It also regulates gastrointestinal motility and intestinal secretion and is thought to be involved in regulating cell growth and differentiation.<ref name="entrez">{{cite web | title = Entrez Gene: HRH2 histamine receptor H2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3274| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hill SJ, Ganellin CR, Timmerman H, ''et al.'' |title=International Union of Pharmacology. XIII. Classification of histamine receptors. |journal=Pharmacol. Rev. |volume=49 |issue= 3 |pages= 253-78 |year= 1997 |pmid= 9311023 |doi= }}
*{{cite journal | author=Del Valle J, Gantz I |title=Novel insights into histamine H2 receptor biology. |journal=Am. J. Physiol. |volume=273 |issue= 5 Pt 1 |pages= G987-96 |year= 1997 |pmid= 9374694 |doi= }}
*{{cite journal | author=Gantz I, Munzert G, Tashiro T, ''et al.'' |title=Molecular cloning of the human histamine H2 receptor. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 3 |pages= 1386-92 |year= 1991 |pmid= 1714721 |doi= }}
*{{cite journal | author=Vannier E, Dinarello CA |title=Histamine enhances interleukin (IL)-1-induced IL-6 gene expression and protein synthesis via H2 receptors in peripheral blood mononuclear cells. |journal=J. Biol. Chem. |volume=269 |issue= 13 |pages= 9952-6 |year= 1994 |pmid= 7511596 |doi= }}
*{{cite journal | author=Smit MJ, Timmerman H, Alewijnse AE, ''et al.'' |title=Visualization of agonist-induced internalization of histamine H2 receptors. |journal=Biochem. Biophys. Res. Commun. |volume=214 |issue= 3 |pages= 1138-45 |year= 1995 |pmid= 7575521 |doi= }}
*{{cite journal | author=Nishi T, Koike T, Oka T, ''et al.'' |title=Identification of the promoter region of the human histamine H2-receptor gene. |journal=Biochem. Biophys. Res. Commun. |volume=210 |issue= 2 |pages= 616-23 |year= 1995 |pmid= 7755641 |doi= 10.1006/bbrc.1995.1703 }}
*{{cite journal | author=Traiffort E, Vizuete ML, Tardivel-Lacombe J, ''et al.'' |title=The guinea pig histamine H2 receptor: gene cloning, tissue expression and chromosomal localization of its human counterpart. |journal=Biochem. Biophys. Res. Commun. |volume=211 |issue= 2 |pages= 570-7 |year= 1995 |pmid= 7794271 |doi= }}
*{{cite journal | author=Orange PR, Heath PR, Wright SR, Pearson RC |title=Allelic variations of the human histamine H2 receptor gene. |journal=Neuroreport |volume=7 |issue= 7 |pages= 1293-6 |year= 1996 |pmid= 8817552 |doi= }}
*{{cite journal | author=Elenkov IJ, Webster E, Papanicolaou DA, ''et al.'' |title=Histamine potently suppresses human IL-12 and stimulates IL-10 production via H2 receptors. |journal=J. Immunol. |volume=161 |issue= 5 |pages= 2586-93 |year= 1998 |pmid= 9725260 |doi= }}
*{{cite journal | author=Murakami H, Sun-Wada GH, Matsumoto M, ''et al.'' |title=Human histamine H2 receptor gene: multiple transcription initiation and tissue-specific expression. |journal=FEBS Lett. |volume=451 |issue= 3 |pages= 327-31 |year= 1999 |pmid= 10371214 |doi= }}
*{{cite journal | author=Wang LD, Wang M, Todisco A, ''et al.'' |title=The human histamine H(2) receptor regulates c-jun and c-fos in a differential manner. |journal=Am. J. Physiol., Cell Physiol. |volume=278 |issue= 6 |pages= C1246-55 |year= 2000 |pmid= 10837353 |doi= }}
*{{cite journal | author=Suh BC, Lee H, Jun DJ, ''et al.'' |title=Inhibition of H2 histamine receptor-mediated cation channel opening by protein kinase C in human promyelocytic cells. |journal=J. Immunol. |volume=167 |issue= 3 |pages= 1663-71 |year= 2001 |pmid= 11466390 |doi= }}
*{{cite journal | author=Brew OB, Sullivan MH |title=Localisation of mRNAs for diamine oxidase and histamine receptors H1 and H2, at the feto-maternal interface of human pregnancy. |journal=Inflamm. Res. |volume=50 |issue= 9 |pages= 449-52 |year= 2002 |pmid= 11603849 |doi= }}
*{{cite journal | author=Shayo C, Fernandez N, Legnazzi BL, ''et al.'' |title=Histamine H2 receptor desensitization: involvement of a select array of G protein-coupled receptor kinases. |journal=Mol. Pharmacol. |volume=60 |issue= 5 |pages= 1049-56 |year= 2001 |pmid= 11641433 |doi= }}
*{{cite journal | author=Tanimoto A, Murata Y, Nomaguchi M, ''et al.'' |title=Histamine increases the expression of LOX-1 via H2 receptor in human monocytic THP-1 cells. |journal=FEBS Lett. |volume=508 |issue= 3 |pages= 345-9 |year= 2001 |pmid= 11728449 |doi= }}
*{{cite journal | author=Gutzmer R, Langer K, Lisewski M, ''et al.'' |title=Expression and function of histamine receptors 1 and 2 on human monocyte-derived dendritic cells. |journal=J. Allergy Clin. Immunol. |volume=109 |issue= 3 |pages= 524-31 |year= 2002 |pmid= 11898002 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Esbenshade TA, Kang CH, Krueger KM, ''et al.'' |title=Differential activation of dual signaling responses by human H1 and H2 histamine receptors. |journal=J. Recept. Signal Transduct. Res. |volume=23 |issue= 1 |pages= 17-31 |year= 2003 |pmid= 12680587 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HSD17B10... {November 20, 2007 11:09:09 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein HSD17B10 image.jpg {November 20, 2007 11:09:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:10:13 PM PST}
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{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HSD17B10_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1so8.
| PDB = {{PDB2|1so8}}, {{PDB2|1u7t}}, {{PDB2|2o23}}
| Name = Hydroxysteroid (17-beta) dehydrogenase 10
| HGNCid = 4800
| Symbol = HSD17B10
| AltSymbols =; 17b-HSD10; ABAD; ERAB; HADH2; HCD2; MHBD; SCHAD
| OMIM = 300256
| ECnumber =
| Homologene = 68403
| MGIid = 1333871
| GeneAtlas_image1 = PBB_GE_HSD17B10_202282_at_tn.png
| Function = {{GNF_GO|id=GO:0003857 |text = 3-hydroxyacyl-CoA dehydrogenase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008709 |text = 7-alpha-hydroxysteroid dehydrogenase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0047015 |text = 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3028
| Hs_Ensembl = ENSG00000072506
| Hs_RefseqProtein = NP_001032900
| Hs_RefseqmRNA = NM_001037811
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 53474931
| Hs_GenLoc_end = 53478045
| Hs_Uniprot = Q99714
| Mm_EntrezGene = 15108
| Mm_Ensembl = ENSMUSG00000025260
| Mm_RefseqmRNA = NM_016763
| Mm_RefseqProtein = NP_058043
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 147342597
| Mm_GenLoc_end = 147345155
| Mm_Uniprot = Q99N15
}}
}}
'''Hydroxysteroid (17-beta) dehydrogenase 10''', also known as '''HSD17B10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HSD17B10 hydroxysteroid (17-beta) dehydrogenase 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3028| 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 3-hydroxyacyl-CoA dehydrogenase type II, a member of the short-chain dehydrogenase/reductase superfamily. The gene product is a mitochondrial protein that catalyzes the oxidation of a wide variety of fatty acids, alcohols, and steroids. The protein has been implicated in the development of Alzheimer's disease, and mutations in the gene are the cause of 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (MHBD). Several alternatively spliced transcript variants have been identified, but the full-length nature of only two transcript variants has been determined.<ref name="entrez">{{cite web | title = Entrez Gene: HSD17B10 hydroxysteroid (17-beta) dehydrogenase 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3028| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yang SY, He XY, Schulz H |title=3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease. |journal=FEBS J. |volume=272 |issue= 19 |pages= 4874-83 |year= 2005 |pmid= 16176262 |doi= 10.1111/j.1742-4658.2005.04911.x }}
*{{cite journal | author=Vredendaal PJ, van den Berg IE, Malingré HE, ''et al.'' |title=Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence. |journal=Biochem. Biophys. Res. Commun. |volume=223 |issue= 3 |pages= 718-23 |year= 1996 |pmid= 8687463 |doi= }}
*{{cite journal | author=Furuta S, Kobayashi A, Miyazawa S, Hashimoto T |title=Cloning and expression of cDNA for a newly identified isozyme of bovine liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria. |journal=Biochim. Biophys. Acta |volume=1350 |issue= 3 |pages= 317-24 |year= 1997 |pmid= 9061028 |doi= }}
*{{cite journal | author=Yan SD, Fu J, Soto C, ''et al.'' |title=An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease. |journal=Nature |volume=389 |issue= 6652 |pages= 689-95 |year= 1997 |pmid= 9338779 |doi= 10.1038/39522 }}
*{{cite journal | author=He XY, Schulz H, Yang SY |title=A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's disease. |journal=J. Biol. Chem. |volume=273 |issue= 17 |pages= 10741-6 |year= 1998 |pmid= 9553139 |doi= }}
*{{cite journal | author=Miller AP, Willard HF |title=Chromosomal basis of X chromosome inactivation: identification of a multigene domain in Xp11.21-p11.22 that escapes X inactivation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 15 |pages= 8709-14 |year= 1998 |pmid= 9671743 |doi= }}
*{{cite journal | author=Sambamurti K, Lahiri DK |title=ERAB contains a putative noncleavable signal peptide. |journal=Biochem. Biophys. Res. Commun. |volume=249 |issue= 2 |pages= 546-9 |year= 1998 |pmid= 9712734 |doi= 10.1006/bbrc.1998.9178 }}
*{{cite journal | author=Hansis C, Jähner D, Spiess AN, ''et al.'' |title=The gene for the Alzheimer-associated beta-amyloid-binding protein (ERAB) is differentially expressed in the testicular Leydig cells of the azoospermic by w/w(v) mouse. |journal=Eur. J. Biochem. |volume=258 |issue= 1 |pages= 53-60 |year= 1998 |pmid= 9851691 |doi= }}
*{{cite journal | author=Yan SD, Shi Y, Zhu A, ''et al.'' |title=Role of ERAB/L-3-hydroxyacyl-coenzyme A dehydrogenase type II activity in Abeta-induced cytotoxicity. |journal=J. Biol. Chem. |volume=274 |issue= 4 |pages= 2145-56 |year= 1999 |pmid= 9890977 |doi= }}
*{{cite journal | author=He XY, Merz G, Mehta P, ''et al.'' |title=Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase. |journal=J. Biol. Chem. |volume=274 |issue= 21 |pages= 15014-9 |year= 1999 |pmid= 10329704 |doi= }}
*{{cite journal | author=Oppermann UC, Salim S, Tjernberg LO, ''et al.'' |title=Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease. |journal=FEBS Lett. |volume=451 |issue= 3 |pages= 238-42 |year= 1999 |pmid= 10371197 |doi= }}
*{{cite journal | author=He XY, Yang YZ, Schulz H, Yang SY |title=Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase. |journal=Biochem. J. |volume=345 Pt 1 |issue= |pages= 139-43 |year= 2000 |pmid= 10600649 |doi= }}
*{{cite journal | author=Yang SY, He XY |title=Role of type 10 17beta-hydroxysteroid dehydrogenase in the pathogenesis of Alzheimer's disease. |journal=Adv. Exp. Med. Biol. |volume=487 |issue= |pages= 101-10 |year= 2001 |pmid= 11403151 |doi= }}
*{{cite journal | author=Frackowiak J, Mazur-Kolecka B, Kaczmarski W, Dickson D |title=Deposition of Alzheimer's vascular amyloid-beta is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB). |journal=Brain Res. |volume=907 |issue= 1-2 |pages= 44-53 |year= 2001 |pmid= 11430884 |doi= }}
*{{cite journal | author=He XY, Merz G, Yang YZ, ''et al.'' |title=Characterization and localization of human type10 17beta-hydroxysteroid dehydrogenase. |journal=Eur. J. Biochem. |volume=268 |issue= 18 |pages= 4899-907 |year= 2001 |pmid= 11559359 |doi= }}
*{{cite journal | author=He XY, Wen GY, Merz G, ''et al.'' |title=Abundant type 10 17 beta-hydroxysteroid dehydrogenase in the hippocampus of mouse Alzheimer's disease model. |journal=Brain Res. Mol. Brain Res. |volume=99 |issue= 1 |pages= 46-53 |year= 2002 |pmid= 11869808 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Ofman R, Ruiter JP, Feenstra M, ''et al.'' |title=2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene. |journal=Am. J. Hum. Genet. |volume=72 |issue= 5 |pages= 1300-7 |year= 2003 |pmid= 12696021 |doi= }}
*{{cite journal | author=Shafqat N, Marschall HU, Filling C, ''et al.'' |title=Expanded substrate screenings of human and Drosophila type 10 17beta-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: characterization of multifunctional 3alpha/7alpha/7beta/17beta/20beta/21-HSD. |journal=Biochem. J. |volume=376 |issue= Pt 1 |pages= 49-60 |year= 2003 |pmid= 12917011 |doi= 10.1042/BJ20030877 }}
*{{cite journal | author=He XY, Yang YZ, Peehl DM, ''et al.'' |title=Oxidative 3alpha-hydroxysteroid dehydrogenase activity of human type 10 17beta-hydroxysteroid dehydrogenase. |journal=J. Steroid Biochem. Mol. Biol. |volume=87 |issue= 2-3 |pages= 191-8 |year= 2004 |pmid= 14672739 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IGFBP6... {November 20, 2007 11:10:52 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein IGFBP6 image.jpg {November 20, 2007 11:11:28 PM PST}
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- INFO: Beginning work on IHH... {November 20, 2007 11:11:48 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein IHH image.jpg {November 20, 2007 11:12:27 PM PST}
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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IHH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1vhh.
| PDB = {{PDB2|1vhh}}
| Name = Indian hedgehog homolog (Drosophila)
| HGNCid = 5956
| Symbol = IHH
| AltSymbols =; BDA1; HHG2
| OMIM = 600726
| ECnumber =
| Homologene = 22586
| MGIid = 96533
| GeneAtlas_image1 = PBB_GE_IHH_215420_at_tn.png
| Function = {{GNF_GO|id=GO:0005113 |text = patched binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}} {{GNF_GO|id=GO:0015485 |text = cholesterol binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0001569 |text = patterning of blood vessels}} {{GNF_GO|id=GO:0001649 |text = osteoblast differentiation}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0016539 |text = intein-mediated protein splicing}} {{GNF_GO|id=GO:0045596 |text = negative regulation of cell differentiation}} {{GNF_GO|id=GO:0048469 |text = cell maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3549
| Hs_Ensembl = ENSG00000163501
| Hs_RefseqProtein = NP_002172
| Hs_RefseqmRNA = NM_002181
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 219628173
| Hs_GenLoc_end = 219633433
| Hs_Uniprot = Q14623
| Mm_EntrezGene = 16147
| Mm_Ensembl = ENSMUSG00000006538
| Mm_RefseqmRNA = NM_010544
| Mm_RefseqProtein = NP_034674
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 74878522
| Mm_GenLoc_end = 74884858
| Mm_Uniprot = Q80XI9
}}
}}
'''Indian hedgehog homolog (Drosophila)''', also known as '''IHH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IHH Indian hedgehog homolog (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3549| 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=Marigo V, Roberts DJ, Lee SM, ''et al.'' |title=Cloning, expression, and chromosomal location of SHH and IHH: two human homologues of the Drosophila segment polarity gene hedgehog. |journal=Genomics |volume=28 |issue= 1 |pages= 44-51 |year= 1995 |pmid= 7590746 |doi= }}
*{{cite journal | author=Chang DT, López A, von Kessler DP, ''et al.'' |title=Products, genetic linkage and limb patterning activity of a murine hedgehog gene. |journal=Development |volume=120 |issue= 11 |pages= 3339-53 |year= 1995 |pmid= 7720571 |doi= }}
*{{cite journal | author=Porter JA, Young KE, Beachy PA |title=Cholesterol modification of hedgehog signaling proteins in animal development. |journal=Science |volume=274 |issue= 5285 |pages= 255-9 |year= 1996 |pmid= 8824192 |doi= }}
*{{cite journal | author=Leek JP, Moynihan TP, Anwar R, ''et al.'' |title=Assignment of Indian hedgehog (IHH) to human chromosome bands 2q33-->q35 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=76 |issue= 3-4 |pages= 187-8 |year= 1997 |pmid= 9186520 |doi= }}
*{{cite journal | author=Pepinsky RB, Zeng C, Wen D, ''et al.'' |title=Identification of a palmitic acid-modified form of human Sonic hedgehog. |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 14037-45 |year= 1998 |pmid= 9593755 |doi= }}
*{{cite journal | author=Carpenter D, Stone DM, Brush J, ''et al.'' |title=Characterization of two patched receptors for the vertebrate hedgehog protein family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 23 |pages= 13630-4 |year= 1998 |pmid= 9811851 |doi= }}
*{{cite journal | author=Chuang PT, McMahon AP |title=Vertebrate Hedgehog signalling modulated by induction of a Hedgehog-binding protein. |journal=Nature |volume=397 |issue= 6720 |pages= 617-21 |year= 1999 |pmid= 10050855 |doi= 10.1038/17611 }}
*{{cite journal | author=Ito H, Akiyama H, Shigeno C, ''et al.'' |title=Hedgehog signaling molecules in bone marrow cells at the initial stage of fracture repair. |journal=Biochem. Biophys. Res. Commun. |volume=262 |issue= 2 |pages= 443-51 |year= 1999 |pmid= 10462495 |doi= 10.1006/bbrc.1999.1197 }}
*{{cite journal | author=Bak M, Hansen C, Friis Henriksen K, Tommerup N |title=The human hedgehog-interacting protein gene: structure and chromosome mapping to 4q31.21-->q31.3. |journal=Cytogenet. Cell Genet. |volume=92 |issue= 3-4 |pages= 300-3 |year= 2001 |pmid= 11435703 |doi= }}
*{{cite journal | author=Gao B, Guo J, She C, ''et al.'' |title=Mutations in IHH, encoding Indian hedgehog, cause brachydactyly type A-1. |journal=Nat. Genet. |volume=28 |issue= 4 |pages= 386-8 |year= 2001 |pmid= 11455389 |doi= 10.1038/ng577 }}
*{{cite journal | author=Gritli-Linde A, Lewis P, McMahon AP, Linde A |title=The whereabouts of a morphogen: direct evidence for short- and graded long-range activity of hedgehog signaling peptides. |journal=Dev. Biol. |volume=236 |issue= 2 |pages= 364-86 |year= 2001 |pmid= 11476578 |doi= 10.1006/dbio.2001.0336 }}
*{{cite journal | author=Kindblom JM, Nilsson O, Hurme T, ''et al.'' |title=Expression and localization of Indian hedgehog (Ihh) and parathyroid hormone related protein (PTHrP) in the human growth plate during pubertal development. |journal=J. Endocrinol. |volume=174 |issue= 2 |pages= R1-6 |year= 2002 |pmid= 12176676 |doi= }}
*{{cite journal | author=Cormier S, Delezoide AL, Benoist-Lasselin C, ''et al.'' |title=Parathyroid hormone receptor type 1/Indian hedgehog expression is preserved in the growth plate of human fetuses affected with fibroblast growth factor receptor type 3 activating mutations. |journal=Am. J. Pathol. |volume=161 |issue= 4 |pages= 1325-35 |year= 2002 |pmid= 12368206 |doi= }}
*{{cite journal | author=McCready ME, Sweeney E, Fryer AE, ''et al.'' |title=A novel mutation in the IHH gene causes brachydactyly type A1: a 95-year-old mystery resolved. |journal=Hum. Genet. |volume=111 |issue= 4-5 |pages= 368-75 |year= 2002 |pmid= 12384778 |doi= 10.1007/s00439-002-0815-2 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Kirkpatrick TJ, Au KS, Mastrobattista JM, ''et al.'' |title=Identification of a mutation in the Indian Hedgehog (IHH) gene causing brachydactyly type A1 and evidence for a third locus. |journal=J. Med. Genet. |volume=40 |issue= 1 |pages= 42-4 |year= 2003 |pmid= 12525541 |doi= }}
*{{cite journal | author=Hellemans J, Coucke PJ, Giedion A, ''et al.'' |title=Homozygous mutations in IHH cause acrocapitofemoral dysplasia, an autosomal recessive disorder with cone-shaped epiphyses in hands and hips. |journal=Am. J. Hum. Genet. |volume=72 |issue= 4 |pages= 1040-6 |year= 2003 |pmid= 12632327 |doi= }}
*{{cite journal | author=Niemann C, Unden AB, Lyle S, ''et al.'' |title=Indian hedgehog and beta-catenin signaling: role in the sebaceous lineage of normal and neoplastic mammalian epidermis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 Suppl 1 |issue= |pages= 11873-80 |year= 2003 |pmid= 12917489 |doi= 10.1073/pnas.1834202100 }}
*{{cite journal | author=Berman DM, Karhadkar SS, Maitra A, ''et al.'' |title=Widespread requirement for Hedgehog ligand stimulation in growth of digestive tract tumours. |journal=Nature |volume=425 |issue= 6960 |pages= 846-51 |year= 2003 |pmid= 14520411 |doi= 10.1038/nature01972 }}
*{{cite journal | author=Garcia-Barceló MM, Lee WS, Sham MH, ''et al.'' |title=Is there a role for the IHH gene in Hirschsprung's disease? |journal=Neurogastroenterol. Motil. |volume=15 |issue= 6 |pages= 663-8 |year= 2004 |pmid= 14651602 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL3RA... {November 20, 2007 11:12:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:13:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Interleukin 3 receptor, alpha (low affinity)
| HGNCid = 6012
| Symbol = IL3RA
| AltSymbols =; CD123; IL3R; IL3RAY; IL3RX; IL3RY; MGC34174; hIL-3Ra
| OMIM = 308385
| ECnumber =
| Homologene = 48088
| MGIid = 96553
| GeneAtlas_image1 = PBB_GE_IL3RA_206148_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004896 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor activity}} {{GNF_GO|id=GO:0004912 |text = interleukin-3 receptor activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3563
| Hs_Ensembl = ENSG00000185291
| Hs_RefseqProtein = NP_002174
| Hs_RefseqmRNA = NM_002183
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 1415509
| Hs_GenLoc_end = 1461581
| Hs_Uniprot = P26951
| Mm_EntrezGene = 16188
| Mm_Ensembl = ENSMUSG00000068758
| Mm_RefseqmRNA = XM_983840
| Mm_RefseqProtein = XP_988934
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 13139762
| Mm_GenLoc_end = 13148759
| Mm_Uniprot = P26952
}}
}}
'''Interleukin 3 receptor, alpha (low affinity)''', also known as '''IL3RA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL3RA interleukin 3 receptor, alpha (low affinity)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3563| 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 interleukin 3 specific subunit of a heterodimeric cytokine receptor. The receptor is comprised of a ligand specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL3 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL3. This gene and the gene encoding the colony stimulating factor 2 receptor alpha chain (CSF2RA) form a cytokine receptor gene cluster in a X-Y pseudoautosomal region on chromosomes X or Y.<ref name="entrez">{{cite web | title = Entrez Gene: IL3RA interleukin 3 receptor, alpha (low affinity)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3563| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hara T, Miyajima A |title=Function and signal transduction mediated by the interleukin 3 receptor system in hematopoiesis. |journal=Stem Cells |volume=14 |issue= 6 |pages= 605-18 |year= 1997 |pmid= 8948019 |doi= }}
*{{cite journal | author=Testa U, Riccioni R, Diverio D, ''et al.'' |title=Interleukin-3 receptor in acute leukemia. |journal=Leukemia |volume=18 |issue= 2 |pages= 219-26 |year= 2004 |pmid= 14671644 |doi= 10.1038/sj.leu.2403224 }}
*{{cite journal | author=Kitamura T, Sato N, Arai K, Miyajima A |title=Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors. |journal=Cell |volume=66 |issue= 6 |pages= 1165-74 |year= 1991 |pmid= 1833064 |doi= }}
*{{cite journal | author=Machide M, Mano H, Todokoro K |title=Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain. |journal=Oncogene |volume=11 |issue= 4 |pages= 619-25 |year= 1995 |pmid= 7651724 |doi= }}
*{{cite journal | author=Yoshimura A, Ohkubo T, Kiguchi T, ''et al.'' |title=A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors. |journal=EMBO J. |volume=14 |issue= 12 |pages= 2816-26 |year= 1995 |pmid= 7796808 |doi= }}
*{{cite journal | author=Kosugi H, Nakagawa Y, Hotta T, ''et al.'' |title=Structure of the gene encoding the alpha subunit of the human interleukin 3 receptor. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 1 |pages= 360-7 |year= 1995 |pmid= 7887951 |doi= 10.1006/bbrc.1995.1346 }}
*{{cite journal | author=Woodcock JM, Zacharakis B, Plaetinck G, ''et al.'' |title=Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF. |journal=EMBO J. |volume=13 |issue= 21 |pages= 5176-85 |year= 1994 |pmid= 7957082 |doi= }}
*{{cite journal | author=Kremer E, Baker E, D'Andrea RJ, ''et al.'' |title=A cytokine receptor gene cluster in the X-Y pseudoautosomal region? |journal=Blood |volume=82 |issue= 1 |pages= 22-8 |year= 1993 |pmid= 8100720 |doi= }}
*{{cite journal | author=Milatovich A, Kitamura T, Miyajima A, Francke U |title=Gene for the alpha-subunit of the human interleukin-3 receptor (IL3RA) localized to the X-Y pseudoautosomal region. |journal=Am. J. Hum. Genet. |volume=53 |issue= 5 |pages= 1146-53 |year= 1993 |pmid= 8213838 |doi= }}
*{{cite journal | author=Macardle PJ, Chen Z, Shih CY, ''et al.'' |title=Characterization of human leucocytes bearing the IL-3 receptor. |journal=Cell. Immunol. |volume=168 |issue= 1 |pages= 59-68 |year= 1996 |pmid= 8599840 |doi= 10.1006/cimm.1996.0049 }}
*{{cite journal | author=Stomski FC, Sun Q, Bagley CJ, ''et al.'' |title=Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding. |journal=Mol. Cell. Biol. |volume=16 |issue= 6 |pages= 3035-46 |year= 1996 |pmid= 8649415 |doi= }}
*{{cite journal | author=Bagley CJ, Phillips J, Cambareri B, ''et al.'' |title=A discontinuous eight-amino acid epitope in human interleukin-3 binds the alpha-chain of its receptor. |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 31922-8 |year= 1997 |pmid= 8943237 |doi= }}
*{{cite journal | author=Klein BK, Feng Y, McWherter CA, ''et al.'' |title=The receptor binding site of human interleukin-3 defined by mutagenesis and molecular modeling. |journal=J. Biol. Chem. |volume=272 |issue= 36 |pages= 22630-41 |year= 1997 |pmid= 9278420 |doi= }}
*{{cite journal | author=Wang P, Wu P, Cheewatrakoolpong B, ''et al.'' |title=Selective inhibition of IL-5 receptor alpha-chain gene transcription by IL-5, IL-3, and granulocyte-macrophage colony-stimulating factor in human blood eosinophils. |journal=J. Immunol. |volume=160 |issue= 9 |pages= 4427-32 |year= 1998 |pmid= 9574547 |doi= }}
*{{cite journal | author=Res PC, Couwenberg F, Vyth-Dreese FA, Spits H |title=Expression of pTalpha mRNA in a committed dendritic cell precursor in the human thymus. |journal=Blood |volume=94 |issue= 8 |pages= 2647-57 |year= 1999 |pmid= 10515868 |doi= }}
*{{cite journal | author=Jahnsen FL, Lund-Johansen F, Dunne JF, ''et al.'' |title=Experimentally induced recruitment of plasmacytoid (CD123high) dendritic cells in human nasal allergy. |journal=J. Immunol. |volume=165 |issue= 7 |pages= 4062-8 |year= 2000 |pmid= 11034417 |doi= }}
*{{cite journal | author=Heinemann A, Hartnell A, Stubbs VE, ''et al.'' |title=Basophil responses to chemokines are regulated by both sequential and cooperative receptor signaling. |journal=J. Immunol. |volume=165 |issue= 12 |pages= 7224-33 |year= 2001 |pmid= 11120855 |doi= }}
*{{cite journal | author=Carr PD, Gustin SE, Church AP, ''et al.'' |title=Structure of the complete extracellular domain of the common beta subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration. |journal=Cell |volume=104 |issue= 2 |pages= 291-300 |year= 2001 |pmid= 11207369 |doi= }}
*{{cite journal | author=Kunitani H, Shimizu Y, Murata H, ''et al.'' |title=Phenotypic analysis of circulating and intrahepatic dendritic cell subsets in patients with chronic liver diseases. |journal=J. Hepatol. |volume=36 |issue= 6 |pages= 734-41 |year= 2002 |pmid= 12044522 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on INPPL1... {November 20, 2007 11:13:31 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:14:13 PM PST}
- CREATED: Created new protein page: INPPL1 {November 20, 2007 11:14:22 PM PST}
- INFO: Beginning work on KCNA2... {November 20, 2007 11:14:22 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein KCNA2 image.jpg {November 20, 2007 11:15:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:15:28 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_KCNA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dsx.
| PDB = {{PDB2|1dsx}}, {{PDB2|1exb}}, {{PDB2|1qdv}}, {{PDB2|1qdw}}, {{PDB2|2a79}}
| Name = Potassium voltage-gated channel, shaker-related subfamily, member 2
| HGNCid = 6220
| Symbol = KCNA2
| AltSymbols =; HK4; HBK5; HUKIV; KV1.2; MGC50217; MK2; NGK1; RBK2
| OMIM = 176262
| ECnumber =
| Homologene = 21034
| MGIid = 96659
| GeneAtlas_image1 = PBB_GE_KCNA2_208564_at_tn.png
| Function = {{GNF_GO|id=GO:0005251 |text = delayed rectifier potassium channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0008076 |text = voltage-gated potassium channel complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3737
| Hs_Ensembl = ENSG00000177301
| Hs_RefseqProtein = NP_004965
| Hs_RefseqmRNA = NM_004974
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 110937725
| Hs_GenLoc_end = 110975619
| Hs_Uniprot = P16389
| Mm_EntrezGene = 16490
| Mm_Ensembl = ENSMUSG00000040724
| Mm_RefseqmRNA = NM_008417
| Mm_RefseqProtein = NP_032443
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 107229623
| Mm_GenLoc_end = 107234935
| Mm_Uniprot = P63141
}}
}}
'''Potassium voltage-gated channel, shaker-related subfamily, member 2''', also known as '''KCNA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNA2 potassium voltage-gated channel, shaker-related subfamily, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3737| 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 = Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the delayed rectifier class, members of which allow nerve cells to efficiently repolarize following an action potential. The coding region of this gene is intronless, and the gene is clustered with genes KCNA3 and KCNA10 on chromosome 1.<ref name="entrez">{{cite web | title = Entrez Gene: KCNA2 potassium voltage-gated channel, shaker-related subfamily, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3737| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gutman GA, Chandy KG, Grissmer S, ''et al.'' |title=International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 473-508 |year= 2006 |pmid= 16382104 |doi= 10.1124/pr.57.4.10 }}
*{{cite journal | author=Paulmichl M, Nasmith P, Hellmiss R, ''et al.'' |title=Cloning and expression of a rat cardiac delayed rectifier potassium channel. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 17 |pages= 7892-5 |year= 1991 |pmid= 1715584 |doi= }}
*{{cite journal | author=Grissmer S, Dethlefs B, Wasmuth JJ, ''et al.'' |title=Expression and chromosomal localization of a lymphocyte K+ channel gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 23 |pages= 9411-5 |year= 1991 |pmid= 2251283 |doi= }}
*{{cite journal | author=McKinnon D |title=Isolation of a cDNA clone coding for a putative second potassium channel indicates the existence of a gene family. |journal=J. Biol. Chem. |volume=264 |issue= 14 |pages= 8230-6 |year= 1989 |pmid= 2722779 |doi= }}
*{{cite journal | author=Kim E, Niethammer M, Rothschild A, ''et al.'' |title=Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases. |journal=Nature |volume=378 |issue= 6552 |pages= 85-8 |year= 1995 |pmid= 7477295 |doi= 10.1038/378085a0 }}
*{{cite journal | author=Klocke R, Roberds SL, Tamkun MM, ''et al.'' |title=Chromosomal mapping in the mouse of eight K(+)-channel genes representing the four Shaker-like subfamilies Shaker, Shab, Shaw, and Shal. |journal=Genomics |volume=18 |issue= 3 |pages= 568-74 |year= 1994 |pmid= 7905852 |doi= }}
*{{cite journal | author=Ramaswami M, Tanouy M, Mathew MK |title=Facile formation of heteromultimeric potassium channels by expression of cloned human cDNAs. |journal=Indian J. Biochem. Biophys. |volume=31 |issue= 4 |pages= 254-60 |year= 1995 |pmid= 8002006 |doi= }}
*{{cite journal | author=Nakahira K, Shi G, Rhodes KJ, Trimmer JS |title=Selective interaction of voltage-gated K+ channel beta-subunits with alpha-subunits. |journal=J. Biol. Chem. |volume=271 |issue= 12 |pages= 7084-9 |year= 1996 |pmid= 8636142 |doi= }}
*{{cite journal | author=Adda S, Fleischmann BK, Freedman BD, ''et al.'' |title=Expression and function of voltage-dependent potassium channel genes in human airway smooth muscle. |journal=J. Biol. Chem. |volume=271 |issue= 22 |pages= 13239-43 |year= 1996 |pmid= 8662756 |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=Kim E, Sheng M |title=Differential K+ channel clustering activity of PSD-95 and SAP97, two related membrane-associated putative guanylate kinases. |journal=Neuropharmacology |volume=35 |issue= 7 |pages= 993-1000 |year= 1997 |pmid= 8938729 |doi= }}
*{{cite journal | author=Cachero TG, Morielli AD, Peralta EG |title=The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel. |journal=Cell |volume=93 |issue= 6 |pages= 1077-85 |year= 1998 |pmid= 9635436 |doi= }}
*{{cite journal | author=Tsai W, Morielli AD, Cachero TG, Peralta EG |title=Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity. |journal=EMBO J. |volume=18 |issue= 1 |pages= 109-18 |year= 1999 |pmid= 9878055 |doi= 10.1093/emboj/18.1.109 }}
*{{cite journal | author=Coleman SK, Newcombe J, Pryke J, Dolly JO |title=Subunit composition of Kv1 channels in human CNS. |journal=J. Neurochem. |volume=73 |issue= 2 |pages= 849-58 |year= 1999 |pmid= 10428084 |doi= }}
*{{cite journal | author=D'Adamo MC, Imbrici P, Sponcichetti F, Pessia M |title=Mutations in the KCNA1 gene associated with episodic ataxia type-1 syndrome impair heteromeric voltage-gated K(+) channel function. |journal=FASEB J. |volume=13 |issue= 11 |pages= 1335-45 |year= 1999 |pmid= 10428758 |doi= }}
*{{cite journal | author=Wade GR, Laurier LG, Preiksaitis HG, Sims SM |title=Delayed rectifier and Ca(2+)-dependent K(+) currents in human esophagus: roles in regulating muscle contraction. |journal=Am. J. Physiol. |volume=277 |issue= 4 Pt 1 |pages= G885-95 |year= 1999 |pmid= 10516156 |doi= }}
*{{cite journal | author=Poliak S, Gollan L, Martinez R, ''et al.'' |title=Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels. |journal=Neuron |volume=24 |issue= 4 |pages= 1037-47 |year= 2000 |pmid= 10624965 |doi= }}
*{{cite journal | author=Manganas LN, Trimmer JS |title=Subunit composition determines Kv1 potassium channel surface expression. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29685-93 |year= 2000 |pmid= 10896669 |doi= 10.1074/jbc.M005010200 }}
*{{cite journal | author=Kuryshev YA, Wible BA, Gudz TI, ''et al.'' |title=KChAP/Kvbeta1.2 interactions and their effects on cardiac Kv channel expression. |journal=Am. J. Physiol., Cell Physiol. |volume=281 |issue= 1 |pages= C290-9 |year= 2001 |pmid= 11401852 |doi= }}
*{{cite journal | author=Byron KL, Lucchesi PA |title=Signal transduction of physiological concentrations of vasopressin in A7r5 vascular smooth muscle cells. A role for PYK2 and tyrosine phosphorylation of K+ channels in the stimulation of Ca2+ spiking. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7298-307 |year= 2002 |pmid= 11739373 |doi= 10.1074/jbc.M104726200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KRT17... {November 20, 2007 11:15:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:16:35 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 = Keratin 17
| HGNCid = 6427
| Symbol = KRT17
| AltSymbols =; PC2; K17; PC; PCHC1
| OMIM = 148069
| ECnumber =
| Homologene = 363
| MGIid = 96691
| GeneAtlas_image1 = PBB_GE_KRT17_205157_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_KRT17_212236_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005882 |text = intermediate filament}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0008544 |text = epidermis development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3872
| Hs_Ensembl = ENSG00000186831
| Hs_RefseqProtein = NP_000413
| Hs_RefseqmRNA = NM_000422
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 37029218
| Hs_GenLoc_end = 37034287
| Hs_Uniprot = Q04695
| Mm_EntrezGene = 16667
| Mm_Ensembl = ENSMUSG00000035557
| Mm_RefseqmRNA = NM_010663
| Mm_RefseqProtein = NP_034793
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 100072305
| Mm_GenLoc_end = 100077079
| Mm_Uniprot = Q9QWL7
}}
}}
'''Keratin 17''', also known as '''KRT17''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KRT17 keratin 17| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3872| 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 = KRT17 encodes the type I intermediate filament chain keratin 17, expressed in nail bed, hair follicle, sebaceous glands, and other epidermal appendages. Mutations in this gene lead to Jackson-Lawler type pachyonychia congenita and steatocystoma multiplex.<ref name="entrez">{{cite web | title = Entrez Gene: KRT17 keratin 17| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3872| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Troyanovsky SM, Leube RE, Franke WW |title=Characterization of the human gene encoding cytokeratin 17 and its expression pattern. |journal=Eur. J. Cell Biol. |volume=59 |issue= 1 |pages= 127-37 |year= 1993 |pmid= 1281771 |doi= }}
*{{cite journal | author=Flohr T, Buwitt U, Bonnekoh B, ''et al.'' |title=Interferon-gamma regulates expression of a novel keratin class I gene. |journal=Eur. J. Immunol. |volume=22 |issue= 4 |pages= 975-9 |year= 1992 |pmid= 1372562 |doi= }}
*{{cite journal | author=Trask DK, Band V, Zajchowski DA, ''et al.'' |title=Keratins as markers that distinguish normal and tumor-derived mammary epithelial cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 6 |pages= 2319-23 |year= 1990 |pmid= 1690428 |doi= }}
*{{cite journal | author=Kartasova T, Cornelissen BJ, Belt P, van de Putte P |title=Effects of UV, 4-NQO and TPA on gene expression in cultured human epidermal keratinocytes. |journal=Nucleic Acids Res. |volume=15 |issue= 15 |pages= 5945-62 |year= 1987 |pmid= 2442723 |doi= }}
*{{cite journal | author=Takahashi K, Folmer J, Coulombe PA |title=Increased expression of keratin 16 causes anomalies in cytoarchitecture and keratinization in transgenic mouse skin. |journal=J. Cell Biol. |volume=127 |issue= 2 |pages= 505-20 |year= 1994 |pmid= 7523421 |doi= }}
*{{cite journal | author=Munro CS, Carter S, Bryce S, ''et al.'' |title=A gene for pachyonychia congenita is closely linked to the keratin gene cluster on 17q12-q21. |journal=J. Med. Genet. |volume=31 |issue= 9 |pages= 675-8 |year= 1995 |pmid= 7529318 |doi= }}
*{{cite journal | author=McLean WH, Rugg EL, Lunny DP, ''et al.'' |title=Keratin 16 and keratin 17 mutations cause pachyonychia congenita. |journal=Nat. Genet. |volume=9 |issue= 3 |pages= 273-8 |year= 1995 |pmid= 7539673 |doi= 10.1038/ng0395-273 }}
*{{cite journal | author=Leigh IM, Navsaria H, Purkis PE, ''et al.'' |title=Keratins (K16 and K17) as markers of keratinocyte hyperproliferation in psoriasis in vivo and in vitro. |journal=Br. J. Dermatol. |volume=133 |issue= 4 |pages= 501-11 |year= 1995 |pmid= 7577575 |doi= }}
*{{cite journal | author=Smith FJ, Corden LD, Rugg EL, ''et al.'' |title=Missense mutations in keratin 17 cause either pachyonychia congenita type 2 or a phenotype resembling steatocystoma multiplex. |journal=J. Invest. Dermatol. |volume=108 |issue= 2 |pages= 220-3 |year= 1997 |pmid= 9008238 |doi= }}
*{{cite journal | author=Covello SP, Smith FJ, Sillevis Smitt JH, ''et al.'' |title=Keratin 17 mutations cause either steatocystoma multiplex or pachyonychia congenita type 2. |journal=Br. J. Dermatol. |volume=139 |issue= 3 |pages= 475-80 |year= 1999 |pmid= 9767294 |doi= }}
*{{cite journal | author=McGowan KM, Coulombe PA |title=Onset of keratin 17 expression coincides with the definition of major epithelial lineages during skin development. |journal=J. Cell Biol. |volume=143 |issue= 2 |pages= 469-86 |year= 1998 |pmid= 9786956 |doi= }}
*{{cite journal | author=Schön M, Benwood J, O'Connell-Willstaedt T, Rheinwald JG |title=Human sweat gland myoepithelial cells express a unique set of cytokeratins and reveal the potential for alternative epithelial and mesenchymal differentiation states in culture. |journal=J. Cell. Sci. |volume=112 ( Pt 12) |issue= |pages= 1925-36 |year= 1999 |pmid= 10341211 |doi= }}
*{{cite journal | author=Celebi JT, Tanzi EL, Yao YJ, ''et al.'' |title=Mutation report: identification of a germline mutation in keratin 17 in a family with pachyonychia congenita type 2. |journal=J. Invest. Dermatol. |volume=113 |issue= 5 |pages= 848-50 |year= 1999 |pmid= 10571744 |doi= 10.1046/j.1523-1747.1999.00762.x }}
*{{cite journal | author=Smith FJ, Coleman CM, Bayoumy NM, ''et al.'' |title=Novel keratin 17 mutations in pachyonychia congenita type 2. |journal=J. Invest. Dermatol. |volume=116 |issue= 5 |pages= 806-8 |year= 2001 |pmid= 11348474 |doi= 10.1046/j.0022-202x.2001.doc.x }}
*{{cite journal | author=Suzuki H, Fukunishi Y, Kagawa I, ''et al.'' |title=Protein-protein interaction panel using mouse full-length cDNAs. |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758-65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101 }}
*{{cite journal | author=Hashiguchi T, Yotsumoto S, Shimada H, ''et al.'' |title=A novel point mutation in the keratin 17 gene in a Japanese case of pachyonychia congenita type 2. |journal=J. Invest. Dermatol. |volume=118 |issue= 3 |pages= 545-7 |year= 2002 |pmid= 11874497 |doi= 10.1046/j.0022-202x.2001.01701.x }}
*{{cite journal | author=Terrinoni A, Smith FJ, Didona B, ''et al.'' |title=Novel and recurrent mutations in the genes encoding keratins K6a, K16 and K17 in 13 cases of pachyonychia congenita. |journal=J. Invest. Dermatol. |volume=117 |issue= 6 |pages= 1391-6 |year= 2002 |pmid= 11886499 |doi= 10.1046/j.0022-202x.2001.01565.x }}
*{{cite journal | author=Scherl A, Couté Y, Déon C, ''et al.'' |title=Functional proteomic analysis of human nucleolus. |journal=Mol. Biol. Cell |volume=13 |issue= 11 |pages= 4100-9 |year= 2003 |pmid= 12429849 |doi= 10.1091/mbc.E02-05-0271 }}
*{{cite journal | author=van de Rijn M, Perou CM, Tibshirani R, ''et al.'' |title=Expression of cytokeratins 17 and 5 identifies a group of breast carcinomas with poor clinical outcome. |journal=Am. J. Pathol. |volume=161 |issue= 6 |pages= 1991-6 |year= 2003 |pmid= 12466114 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LAMP1... {November 20, 2007 11:16:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:18:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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 = Lysosomal-associated membrane protein 1
| HGNCid = 6499
| Symbol = LAMP1
| AltSymbols =; CD107a; LAMPA; LGP120
| OMIM = 153330
| ECnumber =
| Homologene = 4061
| MGIid = 96745
| GeneAtlas_image1 = PBB_GE_LAMP1_201553_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LAMP1_201551_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_LAMP1_201552_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005771 |text = multivesicular body}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0042383 |text = sarcolemma}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3916
| Hs_Ensembl = ENSG00000185896
| Hs_RefseqProtein = NP_005552
| Hs_RefseqmRNA = NM_005561
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 112999557
| Hs_GenLoc_end = 113025746
| Hs_Uniprot = P11279
| Mm_EntrezGene = 16783
| Mm_Ensembl = ENSMUSG00000031447
| Mm_RefseqmRNA = NM_010684
| Mm_RefseqProtein = NP_034814
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 13159138
| Mm_GenLoc_end = 13175307
| Mm_Uniprot = Q3TA96
}}
}}
'''Lysosomal-associated membrane protein 1''', also known as '''LAMP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMP1 lysosomal-associated membrane protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3916| 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 a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands. It may also play a role in tumor cell metastasis.<ref name="entrez">{{cite web | title = Entrez Gene: LAMP1 lysosomal-associated membrane protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3916| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chang MH, Karageorgos LE, Meikle PJ |title=CD107a (LAMP-1) and CD107b (LAMP-2). |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 2 |pages= 147-51 |year= 2003 |pmid= 12144129 |doi= }}
*{{cite journal | author=Schleutker J, Haataja L, Renlund M, ''et al.'' |title=Confirmation of the chromosomal localization of human lamp genes and their exclusion as candidate genes for Salla disease. |journal=Hum. Genet. |volume=88 |issue= 1 |pages= 95-7 |year= 1992 |pmid= 1959930 |doi= }}
*{{cite journal | author=Carlsson SR, Fukuda M |title=The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones. |journal=J. Biol. Chem. |volume=265 |issue= 33 |pages= 20488-95 |year= 1990 |pmid= 2243102 |doi= }}
*{{cite journal | author=Mattei MG, Matterson J, Chen JW, ''et al.'' |title=Two human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2, are encoded by genes localized to chromosome 13q34 and chromosome Xq24-25, respectively. |journal=J. Biol. Chem. |volume=265 |issue= 13 |pages= 7548-51 |year= 1990 |pmid= 2332441 |doi= }}
*{{cite journal | author=Carlsson SR, Fukuda M |title=Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement. |journal=J. Biol. Chem. |volume=264 |issue= 34 |pages= 20526-31 |year= 1990 |pmid= 2584229 |doi= }}
*{{cite journal | author=Mane SM, Marzella L, Bainton DF, ''et al.'' |title=Purification and characterization of human lysosomal membrane glycoproteins. |journal=Arch. Biochem. Biophys. |volume=268 |issue= 1 |pages= 360-78 |year= 1989 |pmid= 2912382 |doi= }}
*{{cite journal | author=Viitala J, Carlsson SR, Siebert PD, Fukuda M |title=Molecular cloning of cDNAs encoding lamp A, a human lysosomal membrane glycoprotein with apparent Mr approximately equal to 120,000. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 11 |pages= 3743-7 |year= 1988 |pmid= 3131762 |doi= }}
*{{cite journal | author=Howe CL, Granger BL, Hull M, ''et al.'' |title=Derived protein sequence, oligosaccharides, and membrane insertion of the 120-kDa lysosomal membrane glycoprotein (lgp120): identification of a highly conserved family of lysosomal membrane glycoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 20 |pages= 7577-81 |year= 1988 |pmid= 3174652 |doi= }}
*{{cite journal | author=Fukuda M, Viitala J, Matteson J, Carlsson SR |title=Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences. |journal=J. Biol. Chem. |volume=263 |issue= 35 |pages= 18920-8 |year= 1989 |pmid= 3198605 |doi= }}
*{{cite journal | author=Ohno H, Stewart J, Fournier MC, ''et al.'' |title=Interaction of tyrosine-based sorting signals with clathrin-associated proteins. |journal=Science |volume=269 |issue= 5232 |pages= 1872-5 |year= 1995 |pmid= 7569928 |doi= }}
*{{cite journal | author=Carlsson SR, Lycksell PO, Fukuda M |title=Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2. |journal=Arch. Biochem. Biophys. |volume=304 |issue= 1 |pages= 65-73 |year= 1993 |pmid= 8323299 |doi= 10.1006/abbi.1993.1322 }}
*{{cite journal | author=Sawada R, Jardine KA, Fukuda M |title=The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-2. 5'-flanking sequence of lamp-2 gene and comparison of exon organization in two genes. |journal=J. Biol. Chem. |volume=268 |issue= 12 |pages= 9014-22 |year= 1993 |pmid= 8517882 |doi= }}
*{{cite journal | author=Rohrer J, Schweizer A, Russell D, Kornfeld S |title=The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. |journal=J. Cell Biol. |volume=132 |issue= 4 |pages= 565-76 |year= 1996 |pmid= 8647888 |doi= }}
*{{cite journal | author=Höning S, Sandoval IV, von Figura K |title=A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. |journal=EMBO J. |volume=17 |issue= 5 |pages= 1304-14 |year= 1998 |pmid= 9482728 |doi= 10.1093/emboj/17.5.1304 }}
*{{cite journal | author=Furuta K, Yang XL, Chen JS, ''et al.'' |title=Differential expression of the lysosome-associated membrane proteins in normal human tissues. |journal=Arch. Biochem. Biophys. |volume=365 |issue= 1 |pages= 75-82 |year= 1999 |pmid= 10222041 |doi= 10.1006/abbi.1999.1147 }}
*{{cite journal | author=Raposo G, Moore M, Innes D, ''et al.'' |title=Human macrophages accumulate HIV-1 particles in MHC II compartments. |journal=Traffic |volume=3 |issue= 10 |pages= 718-29 |year= 2003 |pmid= 12230470 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660-6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
{{refend}}
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