Protein kinase D1

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.[5][6][7]

PRKD1
Identifiers
AliasesPRKD1, PKC-MU, PKCM, PKD, PRKCM, Protein kinase D1, CHDED
External IDsOMIM: 605435 MGI: 99879 HomoloGene: 55680 GeneCards: PRKD1
Orthologs
SpeciesHumanMouse
Entrez

5587

18760

Ensembl

ENSG00000184304

ENSMUSG00000002688

UniProt

Q15139

Q62101

RefSeq (mRNA)

NM_002742
NM_001330069
NM_001348390

NM_008858

RefSeq (protein)

NP_001316998
NP_002733
NP_001335319

NP_032884
NP_001369743
NP_001369744
NP_001369745

Location (UCSC)Chr 14: 29.58 – 30.19 MbChr 12: 50.34 – 50.65 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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][7]

Interactions

Protein kinase D1 has been shown to interact with:

References

  1. GRCh38: Ensembl release 89: ENSG00000184304 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000002688 - 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.
  5. 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. doi:10.1016/S0021-9258(17)37580-4. PMID 8119958.
  6. 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. S2CID 26620985.
  7. "Entrez Gene: PRKD1 protein kinase D1".
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. 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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