PRKCSH

From Wikipedia, the free encyclopedia

Protein kinase C substrate 80K-H

Identifiers

PRKCSH; PLD1; AGE-R2; G19P1; PCLD

External IDs

OMIM: 177060 MGI: 107877 HomoloGene: 2056

Gene ontology
Molecular Function:	• molecular_function • alpha-glucosidase activity • calcium ion binding • protein binding
Cellular Component:	• intracellular • endoplasmic reticulum • alpha-glucosidase II complex
Biological Process:	• protein kinase cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001001329 (mRNA)
NP_001001329 (protein)

NM_008925 (mRNA)
NP_032951 (protein)

Location

Chr 19: 11.41 - 11.42 Mb

Chr 9: 21.75 - 21.76 Mb

Pubmed search

[1]

[2]

Protein kinase C substrate 80K-H, also known as PRKCSH, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PRKCSH protein kinase C substrate 80K-H.

[edit] Further reading

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. PMID 2241894.
Sakai K, Hirai M, Minoshima S, et al. (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. 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. PMID 8125298.
Gress TM, Müller-Pillasch F, Geng M, et al. (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. PMID 8910335.
Ophoff RA, Terwindt GM, Vergouwe MN, et al. (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. PMID 9148925.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Brûlé S, Rabahi F, Faure R, et al. (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. PMID 10684806.
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. 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. PMID 10764838.
Pelletier MF, Marcil A, Sevigny G, et al. (2000). "The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo.". Glycobiology 10 (8): 815–27. PMID 10929008.
Reynolds DM, Falk CT, Li A, et al. (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. PMID 11047756.
Strausberg RL, Feingold EA, Grouse LH, et al. (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. doi:10.1073/pnas.242603899. PMID 12477932.
Li A, Davila S, Furu L, et al. (2003). "Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease.". Am. J. Hum. Genet. 72 (3): 691–703. PMID 12529853.
Drenth JP, te Morsche RH, Smink R, et al. (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.
Gevaert K, Goethals M, Martens L, et al. (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.