PRKCSH

PRKCSH
Identifiers
Aliases	PRKCSH , AGE-R2, G19P1, PCLD, PKCSH, PLD1, GIIB, VASAP-60, protein kinase C substrate 80K-H, PCLD1
External IDs	OMIM: 177060 MGI: 107877 HomoloGene: 2056 GeneCards: PRKCSH
Gene location (Human) Chr. Chromosome 19 (human) [1] Band 19p13.2 Start 11,435,284 bp [1] End 11,450,968 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9 A3|9 8.04 cM Start 21,914,102 bp [2] End 21,925,518 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium olfactory bulb right uterine tube body of pancreas canal of the cervix right lobe of thyroid gland anterior pituitary left lobe of thyroid gland gallbladder body of stomach Top expressed in saccule yolk sac calvaria somite spermatocyte islet of Langerhans left lobe of liver corneal stroma jejunum adrenal gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding phosphoprotein binding transmembrane transporter binding metal ion binding protein kinase C binding protein binding Cellular component endoplasmic reticulum lumen intracellular anatomical structure endoplasmic reticulum glucosidase II complex intracellular membrane-bounded organelle Biological process N-glycan processing intracellular signal transduction post-translational protein modification protein folding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5589 19089 Ensembl ENSG00000130175 ENSMUSG00000003402 UniProt P14314 O08795 RefSeq (mRNA) NM_001001329 NM_001289102 NM_001289103 NM_001289104 NM_002743 NM_001379608 NM_001379609 NM_001293650 NM_001293651 NM_008925 RefSeq (protein) NP_001001329 NP_001276031 NP_001276032 NP_001276033 NP_002734 NP_001366537 NP_001366538 NP_001280579 NP_001280580 NP_032951 Location (UCSC) Chr 19: 11.44 – 11.45 Mb Chr 9: 21.91 – 21.93 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Glucosidase 2 subunit beta is an enzyme that in humans is encoded by the PRKCSH gene. ^[5]

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]

References

1. GRCh38: Ensembl release 89: ENSG00000130175 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000003402 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: PRKCSH protein kinase C substrate 80K-H".

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. 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, 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. 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.