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{{Infobox_gene}}
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'''Protein kinase C eta type''' is an [[enzyme]] that in humans is encoded by the ''PRKCH'' [[gene]].<ref name="pmid1986216">{{cite journal |vauthors=Bacher N, Zisman Y, Berent E, Livneh E | title = Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart | journal = Mol Cell Biol | volume = 11 | issue = 1 | pages = 126–33 |date=Feb 1991 | pmid = 1986216 | pmc = 359602 | doi = }}</ref><ref name="pmid1545821">{{cite journal |vauthors=Bacher N, Zisman Y, Berent E, Livneh E | title = Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart | journal = Mol Cell Biol | volume = 12 | issue = 3 | pages = 1404 |date=Apr 1992 | pmid = 1545821 | pmc = 369574 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRKCH protein kinase C, eta| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5583| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_PRKCH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2fk9.
| PDB = {{PDB2|2fk9}}
| Name = Protein kinase C, eta
| HGNCid = 9403
| Symbol = PRKCH
| AltSymbols =; MGC26269; MGC5363; PKC-L; PKCL; PRKCL; nPKC-eta
| OMIM = 605437
| ECnumber = 
| Homologene = 84384
| MGIid = 97600
| GeneAtlas_image1 = PBB_GE_PRKCH_206099_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKCH_218764_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004697 |text = protein kinase C activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5583
    | Hs_Ensembl = ENSG00000027075
    | Hs_RefseqProtein = NP_006246
    | Hs_RefseqmRNA = NM_006255
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 60858186
    | Hs_GenLoc_end = 61087443
    | Hs_Uniprot = P24723
    | Mm_EntrezGene = 18755
    | Mm_Ensembl = ENSMUSG00000021108
    | Mm_RefseqmRNA = NM_008856
    | Mm_RefseqProtein = NP_032882
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 74503879
    | Mm_GenLoc_end = 74697023
    | Mm_Uniprot = Q3U1I0
  }}
}}
'''Protein kinase C, eta''', also known as '''PRKCH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKCH protein kinase C, eta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5583| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipids-dependent protein kinase. It is predominantly expressed in epithelial tissues and has been shown to reside specifically in the cell nucleus. This protein kinase can regulate keratinocyte differentiation by activating the MAP kinase MAPK13 (p38delta)-activated protein kinase cascade that targets CCAAT/enhancer-binding protein alpha (CEBPA). It is also found to mediate the transcription activation of the transglutaminase 1 (TGM1) gene.<ref name="entrez">{{cite web | title = Entrez Gene: PRKCH protein kinase C, eta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5583| accessdate = }}</ref>
| summary_text = Protein kinase C (PKC) is a family of serine- and threonine-specific [[protein]] kinases that can be activated by [[calcium]] and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipids-dependent protein kinase. It is predominantly expressed in epithelial tissues and has been shown to reside specifically in the cell nucleus. This protein kinase can regulate keratinocyte differentiation by activating the MAP kinase MAPK13 (p38delta)-activated protein kinase cascade that targets CCAAT/enhancer-binding protein alpha (CEBPA). It is also found to mediate the transcription activation of the transglutaminase 1 (TGM1) gene.<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=Greif H, Ben-Chaim J, Shimon T, ''et al.'' |title=The protein kinase C-related PKC-L(eta) gene product is localized in the cell nucleus. |journal=Mol. Cell. Biol. |volume=12 |issue= 3 |pages= 1304-11 |year= 1992 |pmid= 1545811 |doi= }}
*{{cite journal   |vauthors=Greif H, Ben-Chaim J, Shimon T, etal |title=The protein kinase C-related PKC-L(eta) gene product is localized in the cell nucleus. |journal=Mol. Cell. Biol. |volume=12 |issue= 3 |pages= 1304–11 |year= 1992 |pmid= 1545811 |doi= |pmc=369563}}
*{{cite journal  | author=Bacher N, Zisman Y, Berent E, Livneh E |title=Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. |journal=Mol. Cell. Biol. |volume=12 |issue= 3 |pages= 1404 |year= 1992 |pmid= 1545821 |doi= }}
*{{cite journal  |vauthors=Liyanage M, Frith D, Livneh E, Stabel S |title=Protein kinase C group B members PKC-delta, -epsilon, -zeta and PKC-L(eta). Comparison of properties of recombinant proteins in vitro and in vivo. |journal=Biochem. J. |volume=283 |issue= 3|pages= 781–7 |year= 1992 |pmid= 1590767 |doi= |pmc=1130954}}
*{{cite journal  | author=Liyanage M, Frith D, Livneh E, Stabel S |title=Protein kinase C group B members PKC-delta, -epsilon, -zeta and PKC-L(eta). Comparison of properties of recombinant proteins in vitro and in vivo. |journal=Biochem. J. |volume=283 ( Pt 3) |issue= |pages= 781-7 |year= 1992 |pmid= 1590767 |doi=  }}
*{{cite journal  |vauthors=Ruegg CL, Strand M |title=A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1–13 |year= 1991 |pmid= 1832084 |doi=10.1016/0008-8749(91)90051-C }}
*{{cite journal | author=Ruegg CL, Strand M |title=A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1-13 |year= 1991 |pmid= 1832084 |doi=  }}
*{{cite journal   |vauthors=Chowdhury IH, Koyanagi Y, Kobayashi S, etal |title=The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway. |journal=Virology |volume=176 |issue= 1 |pages= 126–32 |year= 1990 |pmid= 1970444 |doi=10.1016/0042-6822(90)90237-L }}
*{{cite journal  | author=Chowdhury IH, Koyanagi Y, Kobayashi S, ''et al.'' |title=The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway. |journal=Virology |volume=176 |issue= 1 |pages= 126-32 |year= 1990 |pmid= 1970444 |doi=  }}
*{{cite journal  |vauthors=Ruegg CL, Strand M |title=Inhibition of protein kinase C and anti-CD3-induced Ca2+ influx in Jurkat T cells by a synthetic peptide with sequence identity to HIV-1 gp41. |journal=J. Immunol. |volume=144 |issue= 10 |pages= 3928–35 |year= 1990 |pmid= 2139676 |doi=  }}
*{{cite journal  | author=Bacher N, Zisman Y, Berent E, Livneh E |title=Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart. |journal=Mol. Cell. Biol. |volume=11 |issue= 1 |pages= 126-33 |year= 1991 |pmid= 1986216 |doi= }}
*{{cite journal  |vauthors=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165–70 |year= 1990 |pmid= 2182321 |doi= |pmc=551792}}
*{{cite journal  | author=Ruegg CL, Strand M |title=Inhibition of protein kinase C and anti-CD3-induced Ca2+ influx in Jurkat T cells by a synthetic peptide with sequence identity to HIV-1 gp41. |journal=J. Immunol. |volume=144 |issue= 10 |pages= 3928-35 |year= 1990 |pmid= 2139676 |doi= }}
*{{cite journal  |vauthors=Fields AP, Bednarik DP, Hess A, May WS |title=Human immunodeficiency virus induces phosphorylation of its cell surface receptor. |journal=Nature |volume=333 |issue= 6170 |pages= 278–80 |year= 1988 |pmid= 3259291 |doi= 10.1038/333278a0 }}
*{{cite journal | author=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165-70 |year= 1990 |pmid= 2182321 |doi= }}
*{{cite journal   |vauthors=Chirmule N, Goonewardena H, Pahwa S, etal |title=HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells. |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19364–9 |year= 1995 |pmid= 7642615 |doi=10.1074/jbc.270.33.19364  }}
*{{cite journal  | author=Fields AP, Bednarik DP, Hess A, May WS |title=Human immunodeficiency virus induces phosphorylation of its cell surface receptor. |journal=Nature |volume=333 |issue= 6170 |pages= 278-80 |year= 1988 |pmid= 3259291 |doi= 10.1038/333278a0 }}
*{{cite journal  |vauthors=Ward NE, Gravitt KR, O'Brian CA |title=Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein. |journal=Cancer Lett. |volume=88 |issue= 1 |pages= 37–40 |year= 1995 |pmid= 7850771 |doi=10.1016/0304-3835(94)03610-U  }}
*{{cite journal  | author=Chirmule N, Goonewardena H, Pahwa S, ''et al.'' |title=HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells. |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19364-9 |year= 1995 |pmid= 7642615 |doi=  }}
*{{cite journal  |vauthors=Palmer RH, Ridden J, Parker PJ |title=Identification of multiple, novel, protein kinase C-related gene products. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 5–8 |year= 1995 |pmid= 7988719 |doi=10.1016/0014-5793(94)01202-4 }}
*{{cite journal  | author=Ward NE, Gravitt KR, O'Brian CA |title=Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein. |journal=Cancer Lett. |volume=88 |issue= 1 |pages= 37-40 |year= 1995 |pmid= 7850771 |doi=  }}
*{{cite journal  |vauthors=Gupta S, Aggarwal S, Kim C, Gollapudi S |title=Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report. |journal=Int. J. Immunopharmacol. |volume=16 |issue= 3 |pages= 197–204 |year= 1994 |pmid= 8206685 |doi=10.1016/0192-0561(94)90013-2 }}
*{{cite journal | author=Palmer RH, Ridden J, Parker PJ |title=Identification of multiple, novel, protein kinase C-related gene products. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 5-8 |year= 1995 |pmid= 7988719 |doi= }}
*{{cite journal   |vauthors=Parada NA, Cruikshank WW, Danis HL, etal |title=IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C. |journal=Cell. Immunol. |volume=168 |issue= 1 |pages= 100–6 |year= 1996 |pmid= 8599832 |doi= 10.1006/cimm.1996.0054 }}
*{{cite journal | author=Gupta S, Aggarwal S, Kim C, Gollapudi S |title=Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report. |journal=Int. J. Immunopharmacol. |volume=16 |issue= 3 |pages= 197-204 |year= 1994 |pmid= 8206685 |doi=  }}
*{{cite journal   |vauthors=Denning MF, Dlugosz AA, Threadgill DW, etal |title=Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5325–31 |year= 1996 |pmid= 8621384 |doi=10.1074/jbc.271.10.5325 }}
*{{cite journal | author=Parada NA, Cruikshank WW, Danis HL, ''et al.'' |title=IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C. |journal=Cell. Immunol. |volume=168 |issue= 1 |pages= 100-6 |year= 1996 |pmid= 8599832 |doi= 10.1006/cimm.1996.0054 }}
*{{cite journal   |vauthors=Ueda E, Ohno S, Kuroki T, etal |title=The eta isoform of protein kinase C mediates transcriptional activation of the human transglutaminase 1 gene. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9790–4 |year= 1996 |pmid= 8621660 |doi=10.1074/jbc.271.16.9790  }}
*{{cite journal  | author=Denning MF, Dlugosz AA, Threadgill DW, ''et al.'' |title=Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5325-31 |year= 1996 |pmid= 8621384 |doi= }}
*{{cite journal  |vauthors=Conant K, Ma M, Nath A, Major EO |title=Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384–9 |year= 1996 |pmid= 8627654 |doi= |pmc=189957}}
*{{cite journal  | author=Ueda E, Ohno S, Kuroki T, ''et al.'' |title=The eta isoform of protein kinase C mediates transcriptional activation of the human transglutaminase 1 gene. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9790-4 |year= 1996 |pmid= 8621660 |doi= }}
*{{cite journal  | author=Holmes AM |title=In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8–12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal  | author=Conant K, Ma M, Nath A, Major EO |title=Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384-9 |year= 1996 |pmid= 8627654 |doi=  }}
*{{cite journal  |vauthors=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332–7 |year= 1998 |pmid= 9446795 |doi=10.1006/bbrc.1997.7877 }}
*{{cite journal | author=Holmes AM |title=In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8-12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal   |vauthors=Zidovetzki R, Wang JL, Chen P, etal |title=Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825–33 |year= 1998 |pmid= 9671211 |doi=10.1089/aid.1998.14.825  }}
*{{cite journal  | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332-7 |year= 1998 |pmid= 9446795 |doi=  }}
*{{cite journal  | author=Zidovetzki R, Wang JL, Chen P, ''et al.'' |title=Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825-33 |year= 1998 |pmid= 9671211 |doi= }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=5583}}
{{Serine/threonine-specific protein kinases}}
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Latest revision as of 18:41, 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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View/Edit Human

Protein kinase C eta type is an enzyme that in humans is encoded by the PRKCH gene.[1][2][3]

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipids-dependent protein kinase. It is predominantly expressed in epithelial tissues and has been shown to reside specifically in the cell nucleus. This protein kinase can regulate keratinocyte differentiation by activating the MAP kinase MAPK13 (p38delta)-activated protein kinase cascade that targets CCAAT/enhancer-binding protein alpha (CEBPA). It is also found to mediate the transcription activation of the transglutaminase 1 (TGM1) gene.[3]

References

  1. ↑ Bacher N, Zisman Y, Berent E, Livneh E (Feb 1991). "Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart". Mol Cell Biol. 11 (1): 126–33. PMC 359602. PMID 1986216.
  2. ↑ Bacher N, Zisman Y, Berent E, Livneh E (Apr 1992). "Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart". Mol Cell Biol. 12 (3): 1404. PMC 369574. PMID 1545821.
  3. ↑ 3.0 3.1 "Entrez Gene: PRKCH protein kinase C, eta".

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=PRKCH&oldid=1416516"