Protein kinase D1

PRKD1

Identifiers

PRKD1, PKC-MU, PKCM, PKD, PRKCM, Protein kinase D1

External IDs

MGI: 99879 HomoloGene: 55680 GeneCards: PRKD1

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 • protein binding • identical protein binding • ATP binding
Cellular component	• cytoplasm • cytosol • Golgi apparatus • membrane • cell-cell junction • plasma membrane • integral component of plasma membrane • trans-Golgi network • cell cortex • nucleus
Biological process	• negative regulation of endocytosis • cell differentiation • intracellular signal transduction • positive regulation of endothelial cell proliferation • regulation of protein stability • Golgi organization • phosphorylation • immune system process • regulation of release of sequestered calcium ion into cytosol • positive regulation of endothelial cell chemotaxis • protein kinase D signaling • sphingolipid biosynthetic process • negative regulation of cell death • nervous system development • positive regulation of peptidyl-serine phosphorylation • positive regulation of angiogenesis • positive regulation of endothelial cell migration • protein phosphorylation • positive regulation of histone deacetylase activity • positive regulation of CREB transcription factor activity • vascular endothelial growth factor receptor signaling pathway • positive regulation of osteoblast differentiation • regulation of integrin-mediated signaling pathway • Golgi vesicle transport • positive regulation of NF-kappaB transcription factor activity • peptidyl-serine phosphorylation • angiogenesis • positive regulation of blood vessel endothelial cell migration • positive regulation of neuron projection development • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway • positive regulation of I-kappaB kinase/NF-kappaB signaling • integrin-mediated signaling pathway • protein autophosphorylation • cellular response to oxidative stress • cellular response to vascular endothelial growth factor stimulus • Ras protein signal transduction • regulation of keratinocyte proliferation • cell proliferation • inflammatory response • innate immune response • signal transduction • positive regulation of transcription from RNA polymerase II promoter • apoptotic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


5587


18760

Ensembl


ENSG00000184304


ENSMUSG00000002688

UniProt


Q15139


Q62101

RefSeq (mRNA)


NM_002742


NM_008858

RefSeq (protein)


NP_002733.2


NP_032884.2

Location (UCSC)

Chr 14: 29.58 – 30.19 Mb

Chr 12: 50.34 – 50.65 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein kinase D1 is an enzyme that in humans is encoded by the PRKD1 gene.^[3]^[4]^[5]

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]^[5]

Interactions

Protein kinase D1 has been shown to interact with:

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
↑ 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.
1 2 "Entrez Gene: PRKD1 protein kinase D1".
↑ 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.
1 2 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.
↑ 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.
↑ 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.
↑ 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.

Van Lint J, Rykx A, Maeda Y, Vantus T, Sturany S, Malhotra V, Vandenheede JR, Seufferlein T (2002). "Protein kinase D: an intracellular traffic regulator on the move". Trends Cell Biol. 12 (4): 193–200. doi:10.1016/S0962-8924(02)02262-6. PMID 11978539.
Busch H, Eisenhart-Rothe BV (1976). "[Old and new dangers of blood transfusion (author's transl)]". MMW, Münchener medizinische Wochenschrift. 118 (22): 713–8. PMID 5668.
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. PMC 551792. PMID 2182321.
Davis RJ, Czech MP (1985). "Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654". Proc. Natl. Acad. Sci. U.S.A. 82 (7): 1974–8. doi:10.1073/pnas.82.7.1974. PMC 397463. PMID 2984676.
Davis RJ, Czech MP (1985). "Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654". Proc. Natl. Acad. Sci. U.S.A. 82 (12): 4080–4. doi:10.1073/pnas.82.12.4080. PMC 397938. PMID 2987962.
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. PMC 189957. PMID 8627654.
Sidorenko SP, Law CL, Klaus SJ, Chandran KA, Takata M, Kurosaki T, Clark EA (1996). "Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling". Immunity. 5 (4): 353–63. doi:10.1016/S1074-7613(00)80261-7. PMID 8885868.
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, Jeyaseelan R, Hofman F (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.
Waldron RT, Iglesias T, Rozengurt E (1999). "The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C". J. Biol. Chem. 274 (14): 9224–30. doi:10.1074/jbc.274.14.9224. PMID 10092595.
Hausser A, Storz P, Link G, Stoll H, Liu YC, Altman A, Pfizenmaier K, Johannes FJ (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.
Jamora C, Yamanouye N, Van Lint J, Laudenslager J, Vandenheede JR, Faulkner DJ, Malhotra V (1999). "Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D". Cell. 98 (1): 59–68. doi:10.1016/S0092-8674(00)80606-6. PMID 10412981.
Bagowski CP, Stein-Gerlach M, Choidas A, Ullrich A (1999). "Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor". EMBO J. 18 (20): 5567–76. doi:10.1093/emboj/18.20.5567. PMC 1171625. PMID 10523301.
Johannes FJ, Hausser A, Storz P, Truckenmüller L, Link G, Kawakami T, Pfizenmaier K (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.
Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ (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.
Mayne M, Holden CP, Nath A, Geiger JD (2000). "Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages". J. Immunol. 164 (12): 6538–42. doi:10.4049/jimmunol.164.12.6538. PMID 10843712.
Matthews SA, Iglesias T, Rozengurt E, Cantrell D (2000). "Spatial and temporal regulation of protein kinase D (PKD)". EMBO J. 19 (12): 2935–45. doi:10.1093/emboj/19.12.2935. PMC 203351. PMID 10856238.
Vertommen D, Rider M, Ni Y, Waelkens E, Merlevede W, Vandenheede JR, Van Lint J (2000). "Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis". J. Biol. Chem. 275 (26): 19567–76. doi:10.1074/jbc.M001357200. PMID 10867018.

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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Protein kinase D1

Function

Interactions

References

Further reading