This gene encodes the beta-subunit of glucosidase II, an N-linked glycan-processing enzyme in the endoplasmic reticulum (ER). This protein is an acidic phospho-protein known to be a substrate for protein kinase C. Mutations in this gene have been associated with the autosomal dominant polycystic liver disease (PCLD). Alternatively spliced transcript variants encoding distinct isoforms have been observed.[5]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000130175 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000003402 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ab"Entrez Gene: PRKCSH protein kinase C substrate 80K-H".
Further readingedit
Thornalley PJ (1999). "Cell activation by glycated proteins. AGE receptors, receptor recognition factors and functional classification of AGEs". Cell. Mol. Biol. (Noisy-le-grand). 44 (7): 1013–23. PMID 9846883.
Lukàcs A (1978). "[Debate on prophylaxis]". Prevenzione Stomatologica. 1 (2): 43–7. PMID 1076483.
Hirai M, Shimizu N (1990). "Purification of two distinct proteins of approximate Mr 80,000 from human epithelial cells and identification as proper substrates for protein kinase C". Biochem. J. 270 (3): 583–9. doi:10.1042/bj2700583. PMC1131772. PMID 2241894.
Sakai K, Hirai M, Minoshima S, Kudoh J, Fukuyama R, Shimizu N (1989). "Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide sequence and chromosomal mapping of the gene for a human 80K protein". Genomics. 5 (2): 309–15. doi:10.1016/0888-7543(89)90063-3. PMID 2793184.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Gress TM, Müller-Pillasch F, Geng M, Zimmerhackl F, Zehetner G, Friess H, Büchler M, Adler G, Lehrach H (1996). "A pancreatic cancer-specific expression profile". Oncogene. 13 (8): 1819–30. PMID 8895530.
Trombetta ES, Simons JF, Helenius A (1996). "Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit". J. Biol. Chem. 271 (44): 27509–16. doi:10.1074/jbc.271.44.27509. PMID 8910335.
Ophoff RA, Terwindt GM, Vergouwe MN, Van Eijk R, Mohrenweiser H, Litt M, Hofker MH, Haan J, Ferrari MD (1997). "A 3-Mb region for the familial hemiplegic migraine locus on 19p13.1-p13.2: exclusion of PRKCSH as a candidate gene. Dutch Migraine Genetic Research Group". Eur. J. Hum. Genet. 4 (6): 321–8. PMID 9043864.
Arendt CW, Ostergaard HL (1997). "Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II". J. Biol. Chem. 272 (20): 13117–25. doi:10.1074/jbc.272.20.13117. PMID 9148925.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Brûlé S, Rabahi F, Faure R, Beckers JF, Silversides DW, Lussier JG (2000). "Vacuolar system-associated protein-60: a protein characterized from bovine granulosa and luteal cells that is associated with intracellular vesicles and related to human 80K-H and murine beta-glucosidase II". Biol. Reprod. 62 (3): 642–54. doi:10.1095/biolreprod62.3.642. hdl:2268/298359. PMID 10684806. S2CID 29259727.
Arendt CW, Ostergaard HL (2000). "Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit". Glycobiology. 10 (5): 487–92. doi:10.1093/glycob/10.5.487. PMID 10764837.
Treml K, Meimaroglou D, Hentges A, Bause E (2000). "The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver". Glycobiology. 10 (5): 493–502. doi:10.1093/glycob/10.5.493. PMID 10764838.
Pelletier MF, Marcil A, Sevigny G, Jakob CA, Tessier DC, Chevet E, Menard R, Bergeron JJ, Thomas DY (2000). "The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo". Glycobiology. 10 (8): 815–27. doi:10.1093/glycob/10.8.815. PMID 10929008.
Reynolds DM, Falk CT, Li A, King B, Kamath P, Hustoniii J, Shub C, Iglesias D, Martin R (2001). "Identification of a Locus for Autosomal Dominant Polycystic Liver Disease, on Chromosome 19p13.2-13.1". Am. J. Hum. Genet. 67 (6): 1598–604. doi:10.1086/316904. PMC1287938. PMID 11047756.
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Li A, Davila S, Furu L, Qian Q, Tian X, Kamath PS, King BF, Torres VE, Somlo S (2003). "Mutations in PRKCSH Cause Isolated Autosomal Dominant Polycystic Liver Disease". Am. J. Hum. Genet. 72 (3): 691–703. doi:10.1086/368295. PMC1180260. PMID 12529853.
Drenth JP, te Morsche RH, Smink R, Bonifacino JS, Jansen JB (2003). "Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease". Nat. Genet. 33 (3): 345–7. doi:10.1038/ng1104. PMID 12577059. S2CID 34672886.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
This article on a gene on human chromosome 19 is a stub. You can help Wikipedia by expanding it.
prkcsh, glucosidase, subunit, beta, enzyme, that, humans, encoded, gene, identifiersaliases, g19p1, pcld, pkcsh, pld1, giib, vasap, protein, kinase, substrate, pcld1external, idsomim, 177060, 107877, homologene, 2056, genecards, gene, location, human, chromoso. Glucosidase 2 subunit beta is an enzyme that in humans is encoded by the PRKCSH gene 5 PRKCSHIdentifiersAliasesPRKCSH AGE R2 G19P1 PCLD PKCSH PLD1 GIIB VASAP 60 protein kinase C substrate 80K H PCLD1External IDsOMIM 177060 MGI 107877 HomoloGene 2056 GeneCards PRKCSHGene location Human Chr Chromosome 19 human 1 Band19p13 2Start11 435 284 bp 1 End11 450 968 bp 1 Gene location Mouse Chr Chromosome 9 mouse 2 Band9 A3 9 8 04 cMStart21 914 102 bp 2 End21 925 518 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed instromal cell of endometriumolfactory bulbright uterine tubebody of pancreascanal of the cervixright lobe of thyroid glandanterior pituitaryleft lobe of thyroid glandgallbladderbody of stomachTop expressed insacculeyolk saccalvariasomitespermatocyteislet of Langerhansleft lobe of livercorneal stromajejunumadrenal glandMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functioncalcium ion binding phosphoprotein binding transmembrane transporter binding metal ion binding protein kinase C binding protein bindingCellular componentendoplasmic reticulum lumen intracellular anatomical structure endoplasmic reticulum glucosidase II complex intracellular membrane bounded organelleBiological processN glycan processing intracellular signal transduction post translational protein modification protein foldingSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez558919089EnsemblENSG00000130175ENSMUSG00000003402UniProtP14314O08795RefSeq mRNA NM 001001329NM 001289102NM 001289103NM 001289104NM 002743NM 001379608NM 001379609NM 001293650NM 001293651NM 008925RefSeq protein NP 001001329NP 001276031NP 001276032NP 001276033NP 002734NP 001366537NP 001366538NP 001280579NP 001280580NP 032951Location UCSC Chr 19 11 44 11 45 MbChr 9 21 91 21 93 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThis gene encodes the beta subunit of glucosidase II an N linked glycan processing enzyme in the endoplasmic reticulum ER This protein is an acidic phospho protein known to be a substrate for protein kinase C Mutations in this gene have been associated with the autosomal dominant polycystic liver disease PCLD Alternatively spliced transcript variants encoding distinct isoforms have been observed 5 References edit a b c GRCh38 Ensembl release 89 ENSG00000130175 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000003402 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b Entrez Gene PRKCSH protein kinase C substrate 80K H Further reading editThornalley PJ 1999 Cell activation by glycated proteins AGE receptors receptor recognition factors and functional classification of AGEs Cell Mol Biol Noisy le grand 44 7 1013 23 PMID 9846883 Lukacs A 1978 Debate on prophylaxis Prevenzione Stomatologica 1 2 43 7 PMID 1076483 Hirai M Shimizu N 1990 Purification of two distinct proteins of approximate Mr 80 000 from human epithelial cells and identification as proper substrates for protein kinase C Biochem J 270 3 583 9 doi 10 1042 bj2700583 PMC 1131772 PMID 2241894 Sakai K Hirai M Minoshima S Kudoh J Fukuyama R Shimizu N 1989 Isolation of cDNAs encoding a substrate for protein kinase C nucleotide sequence and chromosomal mapping of the gene for a human 80K protein Genomics 5 2 309 15 doi 10 1016 0888 7543 89 90063 3 PMID 2793184 Maruyama K Sugano S 1994 Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides Gene 138 1 2 171 4 doi 10 1016 0378 1119 94 90802 8 PMID 8125298 Gress TM Muller Pillasch F Geng M Zimmerhackl F Zehetner G Friess H Buchler M Adler G Lehrach H 1996 A pancreatic cancer specific expression profile Oncogene 13 8 1819 30 PMID 8895530 Trombetta ES Simons JF Helenius A 1996 Endoplasmic reticulum glucosidase II is composed of a catalytic subunit conserved from yeast to mammals and a tightly bound noncatalytic HDEL containing subunit J Biol Chem 271 44 27509 16 doi 10 1074 jbc 271 44 27509 PMID 8910335 Ophoff RA Terwindt GM Vergouwe MN Van Eijk R Mohrenweiser H Litt M Hofker MH Haan J Ferrari MD 1997 A 3 Mb region for the familial hemiplegic migraine locus on 19p13 1 p13 2 exclusion of PRKCSH as a candidate gene Dutch Migraine Genetic Research Group Eur J Hum Genet 4 6 321 8 PMID 9043864 Arendt CW Ostergaard HL 1997 Identification of the CD45 associated 116 kDa and 80 kDa proteins as the alpha and beta subunits of alpha glucosidase II J Biol Chem 272 20 13117 25 doi 10 1074 jbc 272 20 13117 PMID 9148925 Suzuki Y Yoshitomo Nakagawa K Maruyama K Suyama A Sugano S 1997 Construction and characterization of a full length enriched and a 5 end enriched cDNA library Gene 200 1 2 149 56 doi 10 1016 S0378 1119 97 00411 3 PMID 9373149 Brule S Rabahi F Faure R Beckers JF Silversides DW Lussier JG 2000 Vacuolar system associated protein 60 a protein characterized from bovine granulosa and luteal cells that is associated with intracellular vesicles and related to human 80K H and murine beta glucosidase II Biol Reprod 62 3 642 54 doi 10 1095 biolreprod62 3 642 hdl 2268 298359 PMID 10684806 S2CID 29259727 Arendt CW Ostergaard HL 2000 Two distinct domains of the beta subunit of glucosidase II interact with the catalytic alpha subunit Glycobiology 10 5 487 92 doi 10 1093 glycob 10 5 487 PMID 10764837 Treml K Meimaroglou D Hentges A Bause E 2000 The alpha and beta subunits are required for expression of catalytic activity in the hetero dimeric glucosidase II complex from human liver Glycobiology 10 5 493 502 doi 10 1093 glycob 10 5 493 PMID 10764838 Pelletier MF Marcil A Sevigny G Jakob CA Tessier DC Chevet E Menard R Bergeron JJ Thomas DY 2000 The heterodimeric structure of glucosidase II is required for its activity solubility and localization in vivo Glycobiology 10 8 815 27 doi 10 1093 glycob 10 8 815 PMID 10929008 Reynolds DM Falk CT Li A King B Kamath P Hustoniii J Shub C Iglesias D Martin R 2001 Identification of a Locus for Autosomal Dominant Polycystic Liver Disease on Chromosome 19p13 2 13 1 Am J Hum Genet 67 6 1598 604 doi 10 1086 316904 PMC 1287938 PMID 11047756 Strausberg RL Feingold EA Grouse LH Derge JG Klausner RD Collins FS Wagner L Shenmen CM Schuler GD 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Li A Davila S Furu L Qian Q Tian X Kamath PS King BF Torres VE Somlo S 2003 Mutations in PRKCSH Cause Isolated Autosomal Dominant Polycystic Liver Disease Am J Hum Genet 72 3 691 703 doi 10 1086 368295 PMC 1180260 PMID 12529853 Drenth JP te Morsche RH Smink R Bonifacino JS Jansen JB 2003 Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease Nat Genet 33 3 345 7 doi 10 1038 ng1104 PMID 12577059 S2CID 34672886 Gevaert K Goethals M Martens L Van Damme J Staes A Thomas GR Vandekerckhove J 2004 Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N terminal peptides Nat Biotechnol 21 5 566 9 doi 10 1038 nbt810 PMID 12665801 S2CID 23783563 nbsp This article on a gene on human chromosome 19 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title PRKCSH amp oldid 1199622242, wikipedia, wiki, book, books, library,
