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Open Access Articles- Top Results for Protein kinase D1

Protein kinase D1

Template:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/row
Identifiers
SymbolsPRKD1 ; PKC-MU; PKCM; PKD; PRKCM
External IDsOMIM605435 MGI99879 HomoloGene55680 IUPHAR: 1489 ChEMBL: 3863 GeneCards: PRKD1 Gene
EC number2.7.11.13
RNA expression pattern
File:PBB GE PRKD1 205880 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez558718760
EnsemblENSG00000184304ENSMUSG00000002688
UniProtQ15139Q62101
RefSeq (mRNA)NM_002742NM_008858
RefSeq (protein)NP_002733NP_032884
Location (UCSC)Chr 14:
30.05 – 30.66 Mb
Chr 12:
50.34 – 50.65 Mb
PubMed search[1][2]

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. PMID 10965134. doi:10.1159/000015624. 
  3. 3.0 3.1 "Entrez Gene: PRKD1 protein kinase D1". 
  4. Johannes FJ, Hausser A, Storz P, Truckenmüller L, Link G, Kawakami T et al. (November 1999). "Bruton's tyrosine kinase (Btk) associates with protein kinase C mu". FEBS Lett. 461 (1-2): 68–72. PMID 10561498. doi:10.1016/s0014-5793(99)01424-6. 
  5. 5.0 5.1 Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K et al. (August 2000). "Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32". J. Biol. Chem. 275 (32): 24601–7. PMID 10831594. doi:10.1074/jbc.M002964200. 
  6. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI et al. (August 2003). "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C". Biochem. Biophys. Res. Commun. 307 (3): 459–65. PMID 12893243. doi:10.1016/s0006-291x(03)01187-2. 
  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. PMID 14550308. doi:10.1016/j.bbrc.2003.09.118. 
  8. Hausser A, Storz P, Link G, Stoll H, Liu YC, Altman A et al. (April 1999). "Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins". J. Biol. Chem. 274 (14): 9258–64. PMID 10092600. doi:10.1074/jbc.274.14.9258. 

Further reading

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