Serine/threonine-protein kinase D1

Details

Name
Serine/threonine-protein kinase D1
Synonyms
  • 2.7.11.13
  • nPKC-D1
  • nPKC-mu
  • PKD
  • PKD1
  • PRKCM
  • Protein kinase C mu type
  • Protein kinase D
Gene Name
PRKD1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0051928|Serine/threonine-protein kinase D1
MSAPPVLRPPSPLLPVAAAAAAAAAALVPGSGPGPAPFLAPVAAPVGGISFHLQIGLSRE
PVLLLQDSSGDYSLAHVREMACSIVDQKFPECGFYGMYDKILLFRHDPTSENILQLVKAA
SDIQEGDLIEVVLSASATFEDFQIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGC
GLNYHKRCAFKIPNNCSGVRRRRLSNVSLTGVSTIRTSSAELSTSAPDEPLLQKSPSESF
IGREKRSNSQSYIGRPIHLDKILMSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQ
CKDCRFNCHKRCAPKVPNNCLGEVTINGDLLSPGAESDVVMEEGSDDNDSERNSGLMDDM
EEAMVQDAEMAMAECQNDSGEMQDPDPDHEDANRTISPSTSNNIPLMRVVQSVKHTKRKS
STVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPVKTS
ALIPNGANPHCFEITTANVVYYVGENVVNPSSPSPNNSVLTSGVGADVARMWEIAIQHAL
MPVIPKGSSVGTGTNLHRDISVSISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGG
KHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVME
KLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPF
PQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGT
FPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQ
DYQTWLDLRELECKIGERYITHESDDLRWEKYAGEQGLQYPTHLINPSASHSDTPETEET
EMKALGERVSIL
Number of residues
912
Molecular Weight
101703.275
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / identical protein binding / kinase activity / metal ion binding / protein kinase C activity / protein serine/threonine kinase activity
Processes
angiogenesis / apoptotic process / cell proliferation / cellular response to amino acid starvation / cellular response to hydroperoxide / cellular response to oxidative stress / cellular response to vascular endothelial growth factor stimulus / Golgi organization / Golgi vesicle transport / inflammatory response / innate immune response / integrin-mediated signaling pathway / intracellular signal transduction / negative regulation of cell death / negative regulation of endocytosis / peptidyl-serine phosphorylation / peptidyl-threonine phosphorylation / positive regulation of angiogenesis / positive regulation of autophagy / positive regulation of blood vessel endothelial cell migration / positive regulation of CREB transcription factor activity / positive regulation of endothelial cell chemotaxis / positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway / positive regulation of endothelial cell migration / positive regulation of endothelial cell proliferation / positive regulation of histone deacetylase activity / positive regulation of I-kappaB kinase/NF-kappaB signaling / positive regulation of neuron projection development / positive regulation of NF-kappaB transcription factor activity / positive regulation of osteoblast differentiation / positive regulation of peptidyl-serine phosphorylation / positive regulation of phosphatidylinositol 3-kinase activity / positive regulation of transcription by RNA polymerase II / protein autophosphorylation / protein kinase D signaling / protein phosphorylation / Ras protein signal transduction / regulation of integrin-mediated signaling pathway / regulation of keratinocyte proliferation / regulation of protein stability / signal transduction / sphingolipid biosynthetic process / vascular endothelial growth factor receptor signaling pathway
Components
autophagosome membrane / cytosol / Golgi apparatus / integral component of plasma membrane / plasma membrane / trans-Golgi network
General Function
Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. Phosphorylates the epidermal growth factor receptor (EGFR) on dual threonine residues, which leads to the suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition with RAF1 for binding to GTP-bound form of Ras proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric G-protein beta/gamma-subunit complex to maintain the structural integrity of the Golgi membranes, and is required for protein transport along the secretory pathway. In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane. May act by activating the lipid kinase phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local synthesis of phosphorylated inositol lipids, which induces a sequential production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are necessary for membrane fission and generation of specific transport carriers to the cell surface. Under oxidative stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes to cell survival by activating IKK complex and subsequent nuclear translocation and activation of NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3 recycling and promoting its recruitment in newly forming focal adhesion. In osteoblast differentiation, mediates the bone morphogenetic protein 2 (BMP2)-induced nuclear export of HDAC7, which results in the inhibition of HDAC7 transcriptional repression of RUNX2. In neurons, plays an important role in neuronal polarity by regulating the biogenesis of TGN-derived dendritic vesicles, and is involved in the maintenance of dendritic arborization and Golgi structure in hippocampal cells. May potentiate mitogenesis induced by the neuropeptide bombesin or vasopressin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression. Plays an important role in the proliferative response induced by low calcium in keratinocytes, through sustained activation of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a role in cardiac hypertrophy by phosphorylating HDAC5, which in turn triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional activation and induction of downstream target genes that promote myocyte hypertrophy and pathological cardiac remodeling. Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which results in reduced myofilament calcium sensitivity, and accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is also involved in angiogenesis by mediating VEGFA-induced specific subset of gene expression, cell migration, and tube formation. In response to VEGFA, is necessary and required for HDAC7 phosphorylation which induces HDAC7 nuclear export and endothelial cell proliferation and migration. During apoptosis induced by cytarabine and other genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting in activation of its kinase function and increased sensitivity of cells to the cytotoxic effects of genotoxic agents. In epithelial cells, is required for transducing flagellin-stimulated inflammatory responses by binding and phosphorylating TLR5, which contributes to MAPK14/p38 activation and production of inflammatory cytokines. May play a role in inflammatory response by mediating activation of NF-kappa-B. May be involved in pain transmission by directly modulating TRPV1 receptor. Plays a role in activated KRAS-mediated stabilization of ZNF304 in colorectal cancer (CRC) cells (PubMed:24623306). Regulates nuclear translocation of transcription factor TFEB in macrophages upon live S.enterica infection (By similarity).
Specific Function
Atp binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051929|Serine/threonine-protein kinase D1 (PRKD1)
ATGAGCGCCCCTCCGGTCCTGCGGCCGCCCAGTCCGCTGCTGCCCGTGGCGGCGGCAGCT
GCCGCAGCGGCCGCCGCACTGGTCCCAGGGTCCGGGCCCGGGCCCGCGCCGTTCTTGGCT
CCTGTCGCGGCCCCGGTCGGGGGCATCTCGTTCCATCTGCAGATCGGCCTGAGCCGTGAG
CCGGTGCTGCTGCTGCAGGACTCGTCCGGGGACTACAGCCTGGCGCACGTCCGCGAGATG
GCTTGCTCCATTGTCGACCAGAAGTTCCCTGAATGTGGTTTCTACGGAATGTATGATAAG
ATCCTGCTTTTTCGCCATGACCCTACCTCTGAAAACATCCTTCAGCTGGTGAAAGCGGCC
AGTGATATCCAGGAAGGCGATCTTATTGAAGTGGTCTTGTCAGCTTCCGCCACCTTTGAA
GACTTTCAGATTCGTCCCCACGCTCTCTTTGTTCATTCATACAGAGCTCCAGCTTTCTGT
GATCACTGTGGAGAAATGCTGTGGGGGCTGGTACGTCAAGGTCTTAAATGTGAAGGGTGT
GGTCTGAATTACCATAAGAGATGTGCATTTAAAATACCCAACAATTGCAGCGGTGTGAGG
CGGAGAAGGCTCTCAAACGTTTCCCTCACTGGGGTCAGCACCATCCGCACATCATCTGCT
GAACTCTCTACAAGTGCCCCTGATGAGCCCCTTCTGCAAAAATCACCATCAGAGTCGTTT
ATTGGTCGAGAGAAGAGGTCAAATTCTCAATCATACATTGGACGACCAATTCACCTTGAC
AAGATTTTGATGTCTAAAGTTAAAGTGCCGCACACATTTGTCATCCACTCCTACACCCGG
CCCACAGTGTGCCAGTACTGCAAGAAGCTTCTGAAGGGGCTTTTCAGGCAGGGCTTGCAG
TGCAAAGATTGCAGATTCAACTGCCATAAACGTTGTGCACCGAAAGTACCAAACAACTGC
CTTGGCGAAGTGACCATTAATGGAGATTTGCTTAGCCCTGGGGCAGAGTCTGATGTGGTC
ATGGAAGAAGGGAGTGATGACAATGATAGTGAAAGGAACAGTGGGCTCATGGATGATATG
GAAGAAGCAATGGTCCAAGATGCAGAGATGGCAATGGCAGAGTGCCAGAACGACAGTGGC
GAGATGCAAGATCCAGACCCAGACCACGAGGACGCCAACAGAACCATCAGTCCATCAACA
AGCAACAATATCCCACTCATGAGGGTAGTGCAGTCTGTCAAACACACGAAGAGGAAAAGC
AGCACAGTCATGAAAGAAGGATGGATGGTCCACTACACCAGCAAGGACACGCTGCGGAAA
CGGCACTATTGGAGATTGGATAGCAAATGTATTACCCTCTTTCAGAATGACACAGGAAGC
AGGTACTACAAGGAAATTCCTTTATCTGAAATTTTGTCTCTGGAACCAGTAAAAACTTCA
GCTTTAATTCCTAATGGGGCCAATCCTCATTGTTTCGAAATCACTACGGCAAATGTAGTG
TATTATGTGGGAGAAAATGTGGTCAATCCTTCCAGCCCATCACCAAATAACAGTGTTCTC
ACCAGTGGCGTTGGTGCAGATGTGGCCAGGATGTGGGAGATAGCCATCCAGCATGCCCTT
ATGCCCGTCATTCCCAAGGGCTCCTCCGTGGGTACAGGAACCAACTTGCACAGAGATATC
TCTGTGAGTATTTCAGTATCAAATTGCCAGATTCAAGAAAATGTGGACATCAGCACAGTA
TATCAGATTTTTCCTGATGAAGTACTGGGTTCTGGACAGTTTGGAATTGTTTATGGAGGA
AAACATCGTAAAACAGGAAGAGATGTAGCTATTAAAATCATTGACAAATTACGATTTCCA
ACAAAACAAGAAAGCCAGCTTCGTAATGAGGTTGCAATTCTACAGAACCTTCATCACCCT
GGTGTTGTAAATTTGGAGTGTATGTTTGAGACGCCTGAAAGAGTGTTTGTTGTTATGGAA
AAACTCCATGGAGACATGCTGGAAATGATCTTGTCAAGTGAAAAGGGCAGGTTGCCAGAG
CACATAACGAAGTTTTTAATTACTCAGATACTCGTGGCTTTGCGGCACCTTCATTTTAAA
AATATCGTTCACTGTGACCTCAAACCAGAAAATGTGTTGCTAGCCTCAGCTGATCCTTTT
CCTCAGGTGAAACTTTGTGATTTTGGTTTTGCCCGGATCATTGGAGAGAAGTCTTTCCGG
AGGTCAGTGGTGGGTACCCCCGCTTACCTGGCTCCTGAGGTCCTAAGGAACAAGGGCTAC
AATCGCTCTCTAGACATGTGGTCTGTTGGGGTCATCATCTATGTAAGCCTAAGCGGCACA
TTCCCATTTAATGAAGATGAAGACATACACGACCAAATTCAGAATGCAGCTTTCATGTAT
CCACCAAATCCCTGGAAGGAAATATCTCATGAAGCCATTGATCTTATCAACAATTTGCTG
CAAGTAAAAATGAGAAAGCGCTACAGTGTGGATAAGACCTTGAGCCACCCTTGGCTACAG
GACTATCAGACCTGGTTAGATTTGCGAGAGCTGGAATGCAAAATCGGGGAGCGCTACATC
ACCCATGAAAGTGATGACCTGAGGTGGGAGAAGTATGCAGGCGAGCAGGGGCTGCAGTAC
CCCACACACCTGATCAATCCAAGTGCTAGCCACAGTGACACTCCTGAGACTGAAGAAACA
GAAATGAAAGCCCTCGGTGAGCGTGTCAGCATCCTCTGA
Chromosome Location
14
Locus
14q12
External Identifiers
ResourceLink
UniProtKB IDQ15139
UniProtKB Entry NameKPCD1_HUMAN
HGNC IDHGNC:9407
General References
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails
DB11752Bryostatin 1investigationalunknownactivatorDetails