PRKCH: Difference between revisions

PRKCH
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2FK9, 3TXO
Identifiers
Aliases	PRKCH, PKC-L, PKCL, PRKCL, nPKC-eta, protein kinase C eta
External IDs	OMIM: 605437; MGI: 97600; HomoloGene: 84384; GeneCards: PRKCH; OMA:PRKCH - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	61,550,976 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	73,824,959 bp
RNA expression pattern
	Top expressed in
	parotid gland; ; granulocyte; ; blood; ; lymph node; ; tonsil; ; upper lobe of left lung; ; thymus; ; right lung; ; visceral pleura; ; epithelium of colon;
	Top expressed in
	right lung lobe; ; esophagus; ; hair follicle; ; gastrula; ; endothelial cell of lymphatic vessel; ; transitional epithelium of urinary bladder; ; blood; ; thymus; ; lip; ; nucleus accumbens;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; protein kinase C activity; metal ion binding; kinase activity; protein serine/threonine kinase activity; calcium-independent protein kinase C activity; enzyme binding; ATP binding; protein binding;
Cellular component	cytoplasm; cytosol; membrane; cell-cell junction; plasma membrane; extracellular exosome; intracellular anatomical structure;
Biological process	positive regulation of B cell receptor signaling pathway; cell differentiation; intracellular signal transduction; phosphorylation; regulation of bicellular tight junction assembly; positive regulation of keratinocyte differentiation; negative regulation of glial cell apoptotic process; protein kinase C signaling; platelet activation; protein phosphorylation; positive regulation of macrophage derived foam cell differentiation; positive regulation of NF-kappaB transcription factor activity; peptidyl-serine phosphorylation; positive regulation of glial cell proliferation; signal transduction; positive regulation of protein localization to plasma membrane;
	Sources:Amigo / QuickGO
Orthologs
	5583
	18755
	ENSG00000027075
	ENSMUSG00000021108
	P24723
	P23298
	NM_006255
	NM_008856; NM_001313977
	NP_006246
	NP_001300906; NP_032882
	Wikidata
View/Edit Human	View/Edit Mouse

Browse history interactively

← Previous edit

Content deleted Content added

VisualWikitext

Inline

Latest revision as of 05:39, 25 December 2023

Protein kinase C eta type is an enzyme that in humans is encoded by the PRKCH gene.^[5]^[6]^[7]

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.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000027075 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021108 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. doi:10.1128/mcb.11.1.126-133.1991. PMC 359602. PMID 1986216.
^ 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. doi:10.1128/mcb.12.3.1404-.1992. PMC 369574. PMID 1545821.
^ ^a ^b "Entrez Gene: PRKCH protein kinase C, eta".

Greif H, Ben-Chaim J, Shimon T, et al. (1992). "The protein kinase C-related PKC-L(eta) gene product is localized in the cell nucleus". Mol. Cell. Biol. 12 (3): 1304–11. doi:10.1128/mcb.12.3.1304-1311.1992. PMC 369563. PMID 1545811.
Liyanage M, Frith D, Livneh E, Stabel S (1992). "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". Biochem. J. 283 (3): 781–7. doi:10.1042/bj2830781. PMC 1130954. PMID 1590767.
Ruegg CL, Strand M (1991). "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". Cell. Immunol. 137 (1): 1–13. doi:10.1016/0008-8749(91)90051-C. PMID 1832084.
Chowdhury IH, Koyanagi Y, Kobayashi S, et al. (1990). "The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway". Virology. 176 (1): 126–32. doi:10.1016/0042-6822(90)90237-L. PMID 1970444.
Ruegg CL, Strand M (1990). "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". J. Immunol. 144 (10): 3928–35. doi:10.4049/jimmunol.144.10.3928. PMID 2139676.
Jakobovits A, Rosenthal A, Capon DJ (1990). "Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C." EMBO J. 9 (4): 1165–70. doi:10.1002/j.1460-2075.1990.tb08223.x. PMC 551792. PMID 2182321.
Fields AP, Bednarik DP, Hess A, May WS (1988). "Human immunodeficiency virus induces phosphorylation of its cell surface receptor". Nature. 333 (6170): 278–80. Bibcode:1988Natur.333..278F. doi:10.1038/333278a0. PMID 3259291. S2CID 4254146.
Chirmule N, Goonewardena H, Pahwa S, et al. (1995). "HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells". J. Biol. Chem. 270 (33): 19364–9. doi:10.1074/jbc.270.33.19364. PMID 7642615.
Ward NE, Gravitt KR, O'Brian CA (1995). "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". Cancer Lett. 88 (1): 37–40. doi:10.1016/0304-3835(94)03610-U. PMID 7850771.
Palmer RH, Ridden J, Parker PJ (1995). "Identification of multiple, novel, protein kinase C-related gene products". FEBS Lett. 356 (1): 5–8. doi:10.1016/0014-5793(94)01202-4. PMID 7988719.
Gupta S, Aggarwal S, Kim C, Gollapudi S (1994). "Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report". Int. J. Immunopharmacol. 16 (3): 197–204. doi:10.1016/0192-0561(94)90013-2. PMID 8206685.
Parada NA, Cruikshank WW, Danis HL, et al. (1996). "IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C." Cell. Immunol. 168 (1): 100–6. doi:10.1006/cimm.1996.0054. PMID 8599832.
Denning MF, Dlugosz AA, Threadgill DW, et al. (1996). "Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase C delta". J. Biol. Chem. 271 (10): 5325–31. doi:10.1074/jbc.271.10.5325. PMID 8621384.
Ueda E, Ohno S, Kuroki T, et al. (1996). "The eta isoform of protein kinase C mediates transcriptional activation of the human transglutaminase 1 gene". J. Biol. Chem. 271 (16): 9790–4. doi:10.1074/jbc.271.16.9790. PMID 8621660.
Conant K, Ma M, Nath A, Major EO (1996). "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". J. Virol. 70 (3): 1384–9. doi:10.1128/JVI.70.3.1384-1389.1996. PMC 189957. PMID 8627654.
Holmes AM (1996). "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". Arch. Biochem. Biophys. 335 (1): 8–12. doi:10.1006/abbi.1996.0476. PMID 8914829.
Borgatti P, Zauli G, Cantley LC, Capitani S (1998). "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". Biochem. Biophys. Res. Commun. 242 (2): 332–7. doi:10.1006/bbrc.1997.7877. PMID 9446795.
Zidovetzki R, Wang JL, Chen P, et al. (1998). "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". AIDS Res. Hum. Retroviruses. 14 (10): 825–33. doi:10.1089/aid.1998.14.825. PMID 9671211.

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000027075 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021108 – 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.

[pmid1986216-5] 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. doi:10.1128/mcb.11.1.126-133.1991. PMC 359602. PMID 1986216.

[pmid1545821-6] 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. doi:10.1128/mcb.12.3.1404-.1992. PMC 369574. PMID 1545821.

[entrez-7] "Entrez Gene: PRKCH protein kinase C, eta".

[1]

[2]

[3]

[4]

[5]

[6]

[7]

@@ Line 1: / Line 1: @@
+{{cs1 config|name-list-style=vanc}}
-{{PBB|geneid=5583}}
+{{Short description|Protein-coding gene in the species Homo sapiens}}
-'''Protein kinase C eta type''' is an [[enzyme]] that in humans is encoded by the ''PRKCH'' [[gene]].<ref name="pmid1986216">{{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 | month = Feb | pmid = 1986216 | pmc = 359602 | doi =  }}</ref><ref name="pmid1545821">{{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 | month = Apr | pmid = 1545821 | pmc = 369574 | doi =  }}</ref><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>
+{{Infobox_gene}}
+'''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 | doi = 10.1128/mcb.11.1.126-133.1991 | pmid = 1986216 | pmc = 359602 }}</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 | doi = 10.1128/mcb.12.3.1404-.1992 | pmid = 1545821 | pmc = 369574 }}</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}}</ref>
+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"/>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| 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>
-}}
 ==References==
 {{reflist}}
 ==Further reading==
 {{refbegin | 2}}
+*{{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 |doi=10.1128/mcb.12.3.1304-1311.1992 |pmid= 1545811 |pmc=369563}}
-{{PBB_Further_reading
+*{{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 |doi=10.1042/bj2830781 |pmid= 1590767 |pmc=1130954}}
-| 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=  | pmc=369563  }}
+*{{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  |doi-access=free }}
-*{{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=  | pmc=1130954  }}
+*{{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=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  |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 |doi=10.4049/jimmunol.144.10.3928 |pmid= 2139676 |doi-access=free }}
-*{{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=10.1016/0042-6822(90)90237-L  }}
+*{{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= 10.1002/j.1460-2075.1990.tb08223.x|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 |bibcode=1988Natur.333..278F |s2cid=4254146 }}
-*{{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=  10.1029/TC009i005p01165| pmc=551792  | bibcode=1990Tecto...9.1165S  }}
+*{{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  |doi-access=free }}
-*{{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=10.1074/jbc.270.33.19364  }}
+*{{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  |doi-access=free }}
-*{{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=10.1016/0304-3835(94)03610-U  }}
+*{{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=10.1016/0014-5793(94)01202-4  }}
+*{{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 |doi-access= free }}
-*{{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=10.1016/0192-0561(94)90013-2  }}
+*{{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  |doi-access=free }}
-*{{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  |doi-access=free }}
-*{{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=10.1074/jbc.271.10.5325  }}
+*{{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 |doi=10.1128/JVI.70.3.1384-1389.1996 |pmid= 8627654 |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=10.1074/jbc.271.16.9790  }}
-*{{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=  | pmc=189957  }}
 *{{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=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  |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=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=10.1089/aid.1998.14.825  }}
+*{{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  }}
-}}
 {{refend}}
 {{PDB Gallery|geneid=5583}}
-{{gene-14-stub}}
 {{Serine/threonine-specific protein kinases}}
+{{Enzymes}}
+{{Portal bar|Biology|border=no}}
+[[Category:EC 2.7.11]]
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
-{{PBB_Controls
-| update_page = yes
+{{gene-14-stub}}
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)