PRKCSH: Difference between revisions

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{{Infobox_gene}}
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'''Glucosidase 2 subunit beta''' is an [[enzyme]] that in humans is encoded by the ''PRKCSH'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKCSH protein kinase C substrate 80K-H| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5589| accessdate = }}</ref>
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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 = Protein kinase C substrate 80K-H
| HGNCid = 9411
| Symbol = PRKCSH
| AltSymbols =; PLD1; AGE-R2; G19P1; PCLD
| OMIM = 177060
| ECnumber = 
| Homologene = 2056
| MGIid = 107877
| GeneAtlas_image1 = PBB_GE_PRKCSH_200707_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKCSH_214080_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0004558 |text = alpha-glucosidase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0017177 |text = alpha-glucosidase II complex}}
| Process = {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5589
    | Hs_Ensembl = ENSG00000130175
    | Hs_RefseqProtein = NP_001001329
    | Hs_RefseqmRNA = NM_001001329
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 11407269
    | Hs_GenLoc_end = 11422783
    | Hs_Uniprot = P14314
    | Mm_EntrezGene = 19089
    | Mm_Ensembl = ENSMUSG00000003402
    | Mm_RefseqmRNA = NM_008925
    | Mm_RefseqProtein = NP_032951
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 21753437
    | Mm_GenLoc_end = 21764624
    | Mm_Uniprot = Q3TWG2
  }}
}}
'''Protein kinase C substrate 80K-H''', also known as '''PRKCSH''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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.<ref name="entrez">{{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 = }}</ref>
| 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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| 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=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=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  |vauthors=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= | pmc=1131772 }}
*{{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=Sakai K |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=10.1016/0888-7543(89)90063-3 |name-list-format=vanc| author2=Hirai M  | author3=Minoshima S  | display-authors=3  | last4=Kudoh  | first4=J  | last5=Fukuyama  | first5=R  | last6=Shimizu  | first6=N }}
*{{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  |vauthors=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=10.1016/0378-1119(94)90802-8 }}
*{{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=Gress TM |title=A pancreatic cancer-specific expression profile |journal=Oncogene |volume=13 |issue= 8 |pages= 1819–30 |year= 1996 |pmid= 8895530 |doi=  |name-list-format=vanc| author2=Müller-Pillasch F | author3=Geng M  | display-authors=3 | last4=Zimmerhackl  | first4=F  | last5=Zehetner  | first5=G  | last6=Friess  | first6=H  | last7=Büchler  | first7=M  | last8=Adler  | first8=G  | last9=Lehrach  | first9=H }}
*{{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  |vauthors=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=10.1074/jbc.271.44.27509 }}
*{{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=Ophoff RA |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=  |name-list-format=vanc| author2=Terwindt GM  | author3=Vergouwe MN  | display-authors=3  | last4=Van Eijk  | first4=R  | last5=Mohrenweiser  | first5=H | last6=Litt  | first6=M  | last7=Hofker  | first7=MH  | last8=Haan  | first8=J  | last9=Ferrari  | first9=MD }}
*{{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  |vauthors=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=10.1074/jbc.272.20.13117 }}
*{{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=Suzuki Y |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=10.1016/S0378-1119(97)00411-3 |name-list-format=vanc| author2=Yoshitomo-Nakagawa K  | author3=Maruyama K  | display-authors=3  | last4=Suyama  | first4=Akira  | last5=Sugano  | first5=Sumio }}
*{{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=Brûlé S |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=10.1095/biolreprod62.3.642 |name-list-format=vanc| author2=Rabahi F  | author3=Faure R | display-authors=3  | last4=Beckers  | first4=JF  | last5=Silversides  | first5=DW  | last6=Lussier  | first6=JG  }}
*{{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 |vauthors=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=10.1093/glycob/10.5.487  }}
*{{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  |vauthors=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=10.1093/glycob/10.5.493 }}
*{{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=Pelletier MF |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=10.1093/glycob/10.8.815 |name-list-format=vanc| author2=Marcil A  | author3=Sevigny G  | display-authors=3  | last4=Jakob  | first4=CA  | last5=Tessier  | first5=DC  | last6=Chevet  | first6=E  | last7=Menard  | first7=R  | last8=Bergeron  | first8=JJ  | last9=Thomas  | first9=DY  }}
*{{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=Reynolds DM |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=10.1086/316904  | pmc=1287938  |name-list-format=vanc| author2=Falk CT  | author3=Li A  | display-authors=3  | last4=King  | first4=B  | last5=Kamath  | first5=P  | last6=Hustoniii  | first6=J  | last7=Shub  | first7=C  | last8=Iglesias  | first8=D  | last9=Martin  | first9=R  }}
*{{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=Strausberg RL |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  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{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=Li A |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=10.1086/368295  | pmc=1180260  |name-list-format=vanc| author2=Davila S  | author3=Furu L  | display-authors=3  | last4=Qian  | first4=Qi  | last5=Tian  | first5=Xin  | last6=Kamath  | first6=Patrick S.  | last7=King  | first7=Bernard F.  | last8=Torres  | first8=Vicente E.  | last9=Somlo  | first9=Stefan  }}
*{{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=Drenth JP |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  |name-list-format=vanc| author2=te Morsche RH  | author3=Smink R  | display-authors=3  | last4=Bonifacino  | first4=Juan S.  | last5=Jansen  | first5=Jan B.M.J. }}
*{{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 }}
*{{cite journal  | author=Gevaert K |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  |name-list-format=vanc| author2=Goethals M  | author3=Martens L  | display-authors=3  | last4=Van Damme  | first4=Jozef  | last5=Staes  | first5=An  | last6=Thomas  | first6=Grégoire R.  | last7=Vandekerckhove  | first7=Joël }}
}}
}}
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{{protein-stub}}
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{{Sugar hydrolases}}
{{Intracellular signaling peptides and proteins}}
 
 
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[[Category:EF-hand-containing proteins]]

Latest revision as of 18:42, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Glucosidase 2 subunit beta is an enzyme that in humans is encoded by the PRKCSH 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]

References

  1. ↑ 1.0 1.1 "Entrez Gene: PRKCSH protein kinase C substrate 80K-H".

Further reading



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