Protein kinase D1: Difference between revisions

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{{Infobox_gene}}
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'''Serine/threonine-protein kinase D1''' is an [[enzyme]] that in humans is encoded by the ''PRKD1'' [[gene]].<ref name="pmid8119958">{{cite journal | vauthors = Johannes FJ, Prestle J, Eis S, Oberhagemann P, Pfizenmaier K | title = PKCu is a novel, atypical member of the protein kinase C family | journal = J Biol Chem | volume = 269 | issue = 8 | pages = 6140–8 | date = April 1994 | pmid = 8119958 | pmc =  | doi =  }}</ref><ref name="pmid10965134">{{cite journal | vauthors = Owczarek CM, Portbury KJ, Kola I, Hertzog PJ | title = Assignment of protein kinase C mu (PRKCM) to human chromosome band 14q11 with somatic cell hybrids and radiation hybrids | journal = Cytogenet Cell Genet | volume = 89 | issue = 3–4 | pages = 240–1 | date = September 2000 | pmid = 10965134 | pmc = | doi = 10.1159/000015624 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRKD1 protein kinase D1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5587| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Protein kinase D1
| HGNCid = 9407
| Symbol = PRKD1
| AltSymbols =; PKC-MU; PKCM; PKD; PRKCM
| OMIM = 605435
| ECnumber = 
| Homologene = 55680
| MGIid = 99879
| GeneAtlas_image1 = PBB_GE_PRKD1_205880_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004700 |text = atypical protein kinase C activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{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 = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5587
    | Hs_Ensembl = ENSG00000184304
    | Hs_RefseqProtein = NP_002733
    | Hs_RefseqmRNA = NM_002742
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 29116195
    | Hs_GenLoc_end = 29466469
    | Hs_Uniprot = Q15139
    | Mm_EntrezGene = 18760
    | Mm_Ensembl = ENSMUSG00000002688
    | Mm_RefseqmRNA = NM_008858
    | Mm_RefseqProtein = NP_032884
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 51217854
    | Mm_GenLoc_end = 51571105
    | Mm_Uniprot = Q62101
  }}
}}
'''Protein kinase D1''', also known as '''PRKD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKD1 protein kinase D1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5587| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Members of the [[protein kinase D]] (PKD) family function in many extracellular receptor-mediated signal transduction pathways. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface.[supplied by OMIM]<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Members of the protein kinase C (PKC) family function in many extracellular receptor-mediated signal transduction pathways. See PRKCA (MIM 176960) for further background information. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PRKD1 protein kinase D1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5587| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
Protein kinase D1 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[Bruton's tyrosine kinase]],<ref name = pmid10561498>{{cite journal | vauthors = Johannes FJ, Hausser A, Storz P, Truckenmüller L, Link G, Kawakami T, Pfizenmaier K | title = Bruton's tyrosine kinase (Btk) associates with protein kinase C mu | journal = FEBS Lett. | volume = 461 | issue = 1-2 | pages = 68–72 | date = November 1999 | pmid = 10561498 | doi =  10.1016/s0014-5793(99)01424-6}}</ref>
* [[C1QBP]],<ref name = pmid10831594>{{cite journal | vauthors = Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ | title = Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32 | journal = J. Biol. Chem. | volume = 275 | issue = 32 | pages = 24601–7 | date = August 2000 | pmid = 10831594 | doi = 10.1074/jbc.M002964200 }}</ref>
* [[Centaurin, alpha 1]],<ref name = pmid12893243>{{cite journal | vauthors = Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A | title = Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C | journal = Biochem. Biophys. Res. Commun. | volume = 307 | issue = 3 | pages = 459–65 | date = August 2003 | pmid = 12893243 | doi =  10.1016/s0006-291x(03)01187-2}}</ref>
* [[Metallothionein 2A]],<ref name = pmid14550308>{{cite journal | vauthors = Rao PS, Jaggi M, Smith DJ, Hemstreet GP, Balaji KC | title = Metallothionein 2A interacts with the kinase domain of PKCmu in prostate cancer | journal = Biochem. Biophys. Res. Commun. | volume = 310 | issue = 3 | pages = 1032–8 | date = October 2003 | pmid = 14550308 | doi =  10.1016/j.bbrc.2003.09.118}}</ref>  and
* [[YWHAQ]].<ref name = pmid10831594/><ref name = pmid10092600>{{cite journal | vauthors = Hausser A, Storz P, Link G, Stoll H, Liu YC, Altman A, Pfizenmaier K, Johannes FJ | title = Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins | journal = J. Biol. Chem. | volume = 274 | issue = 14 | pages = 9258–64 | date = April 1999 | pmid = 10092600 | doi =  10.1074/jbc.274.14.9258}}</ref>
{{Div col end}}
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Van Lint J, Rykx A, Maeda Y, Vantus T, Sturany S, Malhotra V, Vandenheede JR, Seufferlein T | title = Protein kinase D: an intracellular traffic regulator on the move | journal = Trends Cell Biol. | volume = 12 | issue = 4 | pages = 193–200 | year = 2002 | pmid = 11978539 | doi = 10.1016/S0962-8924(02)02262-6 }}
| citations =
* {{cite journal | vauthors = Busch H, Eisenhart-Rothe BV | title = [Old and new dangers of blood transfusion (author's transl)] | journal = MMW, Münchener medizinische Wochenschrift | volume = 118 | issue = 22 | pages = 713–8 | year = 1976 | pmid = 5668 | doi =  }}
*{{cite journal | author=Van Lint J, Rykx A, Maeda Y, ''et al.'' |title=Protein kinase D: an intracellular traffic regulator on the move. |journal=Trends Cell Biol. |volume=12 |issue= 4 |pages= 193-200 |year= 2002 |pmid= 11978539 |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 | pmc = 551792 | doi =  }}
*{{cite journal | author=Busch H, Eisenhart-Rothe BV |title=[Old and new dangers of blood transfusion (author's transl)] |journal=MMW, Münchener medizinische Wochenschrift |volume=118 |issue= 22 |pages= 713-8 |year= 1976 |pmid= 5668 |doi=  }}
* {{cite journal | vauthors = Davis RJ, Czech MP | title = Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 82 | issue = 7 | pages = 1974–8 | year = 1985 | pmid = 2984676 | pmc = 397463 | doi = 10.1073/pnas.82.7.1974 }}
*{{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 = Davis RJ, Czech MP | title = Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 82 | issue = 12 | pages = 4080–4 | year = 1985 | pmid = 2987962 | pmc = 397938 | doi = 10.1073/pnas.82.12.4080 }}
*{{cite journal | author=Davis RJ, Czech MP |title=Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 7 |pages= 1974-8 |year= 1985 |pmid= 2984676 |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 | pmc = 189957 | doi =  }}
*{{cite journal | author=Davis RJ, Czech MP |title=Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 12 |pages= 4080-4 |year= 1985 |pmid= 2987962 |doi= }}
* {{cite journal | vauthors = Sidorenko SP, Law CL, Klaus SJ, Chandran KA, Takata M, Kurosaki T, Clark EA | title = Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling | journal = Immunity | volume = 5 | issue = 4 | pages = 353–63 | year = 1996 | pmid = 8885868 | doi = 10.1016/S1074-7613(00)80261-7 }}
*{{cite journal | author=Johannes FJ, Prestle J, Eis S, ''et al.'' |title=PKCu is a novel, atypical member of the protein kinase C family. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 6140-8 |year= 1994 |pmid= 8119958 |doi=  }}
* {{cite journal | vauthors = 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=Sidorenko SP, Law CL, Klaus SJ, ''et al.'' |title=Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling. |journal=Immunity |volume=5 |issue= 4 |pages= 353-63 |year= 1996 |pmid= 8885868 |doi= }}
* {{cite journal | vauthors = Zidovetzki R, Wang JL, Chen P, Jeyaseelan R, Hofman F | 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=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 = Waldron RT, Iglesias T, Rozengurt E | title = The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C | journal = J. Biol. Chem. | volume = 274 | issue = 14 | pages = 9224–30 | year = 1999 | pmid = 10092595 | doi = 10.1074/jbc.274.14.9224 }}
*{{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 | vauthors = Hausser A, Storz P, Link G, Stoll H, Liu YC, Altman A, Pfizenmaier K, Johannes FJ | title = Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins | journal = J. Biol. Chem. | volume = 274 | issue = 14 | pages = 9258–64 | year = 1999 | pmid = 10092600 | doi = 10.1074/jbc.274.14.9258 }}
*{{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= }}
* {{cite journal | vauthors = Jamora C, Yamanouye N, Van Lint J, Laudenslager J, Vandenheede JR, Faulkner DJ, Malhotra V | title = Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D | journal = Cell | volume = 98 | issue = 1 | pages = 59–68 | year = 1999 | pmid = 10412981 | doi = 10.1016/S0092-8674(00)80606-6 }}
*{{cite journal | author=Waldron RT, Iglesias T, Rozengurt E |title=The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9224-30 |year= 1999 |pmid= 10092595 |doi= }}
* {{cite journal | vauthors = Bagowski CP, Stein-Gerlach M, Choidas A, Ullrich A | title = Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor | journal = EMBO J. | volume = 18 | issue = 20 | pages = 5567–76 | year = 1999 | pmid = 10523301 | pmc = 1171625 | doi = 10.1093/emboj/18.20.5567 }}
*{{cite journal | author=Hausser A, Storz P, Link G, ''et al.'' |title=Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9258-64 |year= 1999 |pmid= 10092600 |doi= }}
* {{cite journal | vauthors = Johannes FJ, Hausser A, Storz P, Truckenmüller L, Link G, Kawakami T, Pfizenmaier K | title = Bruton's tyrosine kinase (Btk) associates with protein kinase C mu | journal = FEBS Lett. | volume = 461 | issue = 1–2 | pages = 68–72 | year = 1999 | pmid = 10561498 | doi = 10.1016/S0014-5793(99)01424-6 }}
*{{cite journal | author=Jamora C, Yamanouye N, Van Lint J, ''et al.'' |title=Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D. |journal=Cell |volume=98 |issue= 1 |pages= 59-68 |year= 1999 |pmid= 10412981 |doi= 10.1016/S0092-8674(00)80606-6 }}
* {{cite journal | vauthors = Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ | title = Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32 | journal = J. Biol. Chem. | volume = 275 | issue = 32 | pages = 24601–7 | year = 2000 | pmid = 10831594 | doi = 10.1074/jbc.M002964200 }}
*{{cite journal | author=Bagowski CP, Stein-Gerlach M, Choidas A, Ullrich A |title=Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor. |journal=EMBO J. |volume=18 |issue= 20 |pages= 5567-76 |year= 1999 |pmid= 10523301 |doi= 10.1093/emboj/18.20.5567 }}
* {{cite journal | vauthors = Mayne M, Holden CP, Nath A, Geiger JD | title = Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages | journal = J. Immunol. | volume = 164 | issue = 12 | pages = 6538–42 | year = 2000 | pmid = 10843712 | doi = 10.4049/jimmunol.164.12.6538 }}
*{{cite journal | author=Johannes FJ, Hausser A, Storz P, ''et al.'' |title=Bruton's tyrosine kinase (Btk) associates with protein kinase C mu. |journal=FEBS Lett. |volume=461 |issue= 1-2 |pages= 68-72 |year= 1999 |pmid= 10561498 |doi= }}
* {{cite journal | vauthors = Matthews SA, Iglesias T, Rozengurt E, Cantrell D | title = Spatial and temporal regulation of protein kinase D (PKD) | journal = EMBO J. | volume = 19 | issue = 12 | pages = 2935–45 | year = 2000 | pmid = 10856238 | pmc = 203351 | doi = 10.1093/emboj/19.12.2935 }}
*{{cite journal | author=Storz P, Hausser A, Link G, ''et al.'' |title=Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24601-7 |year= 2000 |pmid= 10831594 |doi= 10.1074/jbc.M002964200 }}
* {{cite journal | vauthors = Vertommen D, Rider M, Ni Y, Waelkens E, Merlevede W, Vandenheede JR, Van Lint J | title = Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis | journal = J. Biol. Chem. | volume = 275 | issue = 26 | pages = 19567–76 | year = 2000 | pmid = 10867018 | doi = 10.1074/jbc.M001357200 }}
*{{cite journal | author=Mayne M, Holden CP, Nath A, Geiger JD |title=Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages. |journal=J. Immunol. |volume=164 |issue= 12 |pages= 6538-42 |year= 2000 |pmid= 10843712 |doi= }}
*{{cite journal | author=Matthews SA, Iglesias T, Rozengurt E, Cantrell D |title=Spatial and temporal regulation of protein kinase D (PKD). |journal=EMBO J. |volume=19 |issue= 12 |pages= 2935-45 |year= 2000 |pmid= 10856238 |doi= 10.1093/emboj/19.12.2935 }}
*{{cite journal  | author=Vertommen D, Rider M, Ni Y, ''et al.'' |title=Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19567-76 |year= 2000 |pmid= 10867018 |doi= 10.1074/jbc.M001357200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
 
{{gene-14-stub}}
 
[[Category:EC 2.7.11]]

Latest revision as of 15:31, 8 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

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.[1][2][3]

Function

Members of the protein kinase D (PKD) family function in many extracellular receptor-mediated signal transduction pathways. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface.[supplied by OMIM][3]

Interactions

Protein kinase D1 has been shown to interact with:

References

  1. ↑ Johannes FJ, Prestle J, Eis S, Oberhagemann P, Pfizenmaier K (April 1994). "PKCu is a novel, atypical member of the protein kinase C family". J Biol Chem. 269 (8): 6140–8. PMID 8119958.
  2. ↑ Owczarek CM, Portbury KJ, Kola I, Hertzog PJ (September 2000). "Assignment of protein kinase C mu (PRKCM) to human chromosome band 14q11 with somatic cell hybrids and radiation hybrids". Cytogenet Cell Genet. 89 (3–4): 240–1. doi:10.1159/000015624. PMID 10965134.
  3. ↑ 3.0 3.1 "Entrez Gene: PRKD1 protein kinase D1".
  4. ↑ Johannes FJ, Hausser A, Storz P, Truckenmüller L, Link G, Kawakami T, Pfizenmaier K (November 1999). "Bruton's tyrosine kinase (Btk) associates with protein kinase C mu". FEBS Lett. 461 (1–2): 68–72. doi:10.1016/s0014-5793(99)01424-6. PMID 10561498.
  5. ↑ 5.0 5.1 Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ (August 2000). "Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32". J. Biol. Chem. 275 (32): 24601–7. doi:10.1074/jbc.M002964200. PMID 10831594.
  6. ↑ Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A (August 2003). "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C". Biochem. Biophys. Res. Commun. 307 (3): 459–65. doi:10.1016/s0006-291x(03)01187-2. PMID 12893243.
  7. ↑ Rao PS, Jaggi M, Smith DJ, Hemstreet GP, Balaji KC (October 2003). "Metallothionein 2A interacts with the kinase domain of PKCmu in prostate cancer". Biochem. Biophys. Res. Commun. 310 (3): 1032–8. doi:10.1016/j.bbrc.2003.09.118. PMID 14550308.
  8. ↑ Hausser A, Storz P, Link G, Stoll H, Liu YC, Altman A, Pfizenmaier K, Johannes FJ (April 1999). "Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins". J. Biol. Chem. 274 (14): 9258–64. doi:10.1074/jbc.274.14.9258. PMID 10092600.

Further reading


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