PRKCSH

Protein kinase C substrate 80K-H, also known as PRKCSH, is a human gene.cite web | title = Entrez Gene: PRKCSH protein kinase C substrate 80K-H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5589| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: PRKCSH protein kinase C substrate 80K-H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5589| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Thornalley PJ |title=Cell activation by glycated proteins. AGE receptors, receptor recognition factors and functional classification of AGEs. |journal=Cell. Mol. Biol. (Noisy-le-grand) |volume=44 |issue= 7 |pages= 1013–23 |year= 1999 |pmid= 9846883 |doi=
*cite journal | author=Lukàcs A |title= [Debate on prophylaxis] |journal=Prevenzione stomatologica |volume=1 |issue= 2 |pages= 43–7 |year= 1978 |pmid= 1076483 |doi=
*cite journal | author=Hirai M, Shimizu N |title=Purification of two distinct proteins of approximate Mr 80,000 from human epithelial cells and identification as proper substrates for protein kinase C. |journal=Biochem. J. |volume=270 |issue= 3 |pages= 583–9 |year= 1990 |pmid= 2241894 |doi=
*cite journal | author=Sakai K, Hirai M, Minoshima S, "et al." |title=Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide sequence and chromosomal mapping of the gene for a human 80K protein. |journal=Genomics |volume=5 |issue= 2 |pages= 309–15 |year= 1989 |pmid= 2793184 |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=Gress TM, Müller-Pillasch F, Geng M, "et al." |title=A pancreatic cancer-specific expression profile. |journal=Oncogene |volume=13 |issue= 8 |pages= 1819–30 |year= 1996 |pmid= 8895530 |doi=
*cite journal | author=Trombetta ES, Simons JF, Helenius A |title=Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27509–16 |year= 1996 |pmid= 8910335 |doi=
*cite journal | author=Ophoff RA, Terwindt GM, Vergouwe MN, "et al." |title=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. |journal=Eur. J. Hum. Genet. |volume=4 |issue= 6 |pages= 321–8 |year= 1997 |pmid= 9043864 |doi=
*cite journal | author=Arendt CW, Ostergaard HL |title=Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13117–25 |year= 1997 |pmid= 9148925 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Brûlé S, Rabahi F, Faure R, "et al." |title=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. |journal=Biol. Reprod. |volume=62 |issue= 3 |pages= 642–54 |year= 2000 |pmid= 10684806 |doi=
*cite journal | author=Arendt CW, Ostergaard HL |title=Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit. |journal=Glycobiology |volume=10 |issue= 5 |pages= 487–92 |year= 2000 |pmid= 10764837 |doi=
*cite journal | author=Treml K, Meimaroglou D, Hentges A, Bause E |title=The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver. |journal=Glycobiology |volume=10 |issue= 5 |pages= 493–502 |year= 2000 |pmid= 10764838 |doi=
*cite journal | author=Pelletier MF, Marcil A, Sevigny G, "et al." |title=The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. |journal=Glycobiology |volume=10 |issue= 8 |pages= 815–27 |year= 2000 |pmid= 10929008 |doi=
*cite journal | author=Reynolds DM, Falk CT, Li A, "et al." |title=Identification of a locus for autosomal dominant polycystic liver disease, on chromosome 19p13.2-13.1. |journal=Am. J. Hum. Genet. |volume=67 |issue= 6 |pages= 1598–604 |year= 2001 |pmid= 11047756 |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=Li A, Davila S, Furu L, "et al." |title=Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease. |journal=Am. J. Hum. Genet. |volume=72 |issue= 3 |pages= 691–703 |year= 2003 |pmid= 12529853 |doi=
*cite journal | author=Drenth JP, te Morsche RH, Smink R, "et al." |title=Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease. |journal=Nat. Genet. |volume=33 |issue= 3 |pages= 345–7 |year= 2003 |pmid= 12577059 |doi= 10.1038/ng1104
*cite journal | author=Gevaert K, Goethals M, Martens L, "et al." |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810

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