Contents

PRKD2

Protein-coding gene in the species Homo sapiens

PRKD2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2COA, 3BGM, 4NNX, 4NNY
Identifiers
Aliases	PRKD2, PKD2, nPKC-D2, HSPC187, protein kinase D2
External IDs	OMIM: 607074; MGI: 2141917; HomoloGene: 9516; GeneCards: PRKD2; OMA:PRKD2 - orthologs
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19q13.32 Start 46,674,275 bp[1] End 46,717,127 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 A2 Start 16,576,827 bp[2] End 16,604,389 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in vena cava superficial temporal artery Skeletal muscle tissue of rectus abdominis granulocyte spleen body of tongue pylorus lactiferous duct cardia skin of leg Top expressed in thymus granulocyte mesenteric lymph nodes spleen blood primary oocyte right lung right lung lobe left lung external carotid artery More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity protein kinase activity nucleotide binding protein kinase C activity metal ion binding kinase activity protein binding ATP binding protein serine/threonine kinase activity protein kinase C binding Cellular component cytoplasm Golgi apparatus membrane nucleoplasm nucleus cytosol plasma membrane intracellular anatomical structure Biological process positive regulation of vascular endothelial growth factor receptor signaling pathway intracellular signal transduction positive regulation of endothelial cell proliferation adaptive immune response phosphorylation immune system process endothelial tube morphogenesis positive regulation of fibroblast growth factor receptor signaling pathway positive regulation of T cell receptor signaling pathway positive regulation of endothelial cell chemotaxis positive regulation of DNA-binding transcription factor activity cell death protein kinase D signaling positive regulation of intracellular signal transduction 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 cell adhesion positive regulation of NF-kappaB transcription factor activity positive regulation of interleukin-2 production angiogenesis positive regulation of interleukin-8 production positive regulation of blood vessel endothelial cell migration positive regulation of DNA biosynthetic process positive regulation of ERK1 and ERK2 cascade positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway protein autophosphorylation cellular response to vascular endothelial growth factor stimulus T cell receptor signaling pathway positive regulation of transcription by RNA polymerase II positive regulation of cell adhesion sphingolipid biosynthetic process peptidyl-serine phosphorylation peptidyl-threonine phosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 25865 101540 Ensembl ENSG00000105287 ENSMUSG00000041187 UniProt Q9BZL6 Q8BZ03 RefSeq (mRNA) NM_001079880 NM_001079881 NM_001079882 NM_016457 NM_001252458 NM_178900 RefSeq (protein) NP_001073349 NP_001073350 NP_001073351 NP_057541 NP_001239387 NP_849231 Location (UCSC) Chr 19: 46.67 – 46.72 Mb Chr 7: 16.58 – 16.6 Mb PubMed search [3] [4]
Wikidata
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Serine/threonine-protein kinase D2 or PKD2 is an enzyme that in humans is encoded by the PRKD2 gene.^[5][6][7]

Function[edit]

The protein encoded by this gene belongs to the protein kinase D (PKD) family of serine/threonine protein kinases, a subfamily of protein kinase C. This kinase can be activated by phorbol esters as well as by gastrin via the cholecystokinin B receptor (CCKBR) in gastric cancer cells. It can bind to diacylglycerol (DAG) in the trans-Golgi network (TGN) and may regulate basolateral membrane protein exit from TGN. Alternative splicing results in multiple transcript variants encoding different isoforms.^[7]

References[edit]

Further reading[edit]

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