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PRKD1 (Serine/threonine-protein kinase D1) is a protein kinase, an enzyme that switches other proteins on by adding phosphate groups. The public catalogues list it as a drug target, an oncogene driver and a tumour suppressor, and an approved or late-stage drug is recorded against it. Tied to Leukaemia, Myeloproliferative neoplasms, Colorectal cancer and 4 more.
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 signalling, 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) signalling, 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).
Open Targets scores its association with cancer at 0.68 (direct and indirect evidence; datatypes literature 0.95, genetic association 0.41, somatic mutation 0.46, clinical 0.92). IntOGen calls it a driver in 3 cohorts (2 activating, 1 loss-of-function), covering Cholangiocarcinoma, Colorectal Adenocarcinoma, Prostate Adenocarcinoma.
In plain words · PRKD1 (Serine/threonine-protein kinase D1) is a protein kinase, an enzyme that switches other proteins on by adding phosphate groups. The public catalogues list it as a drug target, an oncogene driver and a tumour suppressor, and an approved or late-stage drug is recorded against it. Tied to Leukaemia, Myeloproliferative neoplasms, Colorectal cancer and 4 more.
PRKD1 (Serine/threonine-protein kinase D1) is a protein kinase, an enzyme that switches other proteins on by adding phosphate groups. The public catalogues list it as a drug target, an oncogene driver and a tumour suppressor, and an approved or late-stage drug is recorded against it. Tied to Leukaemia, Myeloproliferative neoplasms, Colorectal cancer and 4 more.
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 signalling, 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) signalling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response.
No product in this corpus aims at PRKD1 yet. Kinases are switched on by binding ATP inside the cell, so most drugs are small molecules shaped to plug that ATP pocket.
Tumour-specific alteration: the catalogues call it an oncogene driver (IntOGen cohort analysis finds it activated more often than chance) and a tumour suppressor (IntOGen finds it knocked out more often than chance), so the direction differs between cohorts but the alteration is somatic either way; what a medicine would aim at or exploit is the altered form or its loss, absent from normal cells; no corpus medicine is aimed at it yet. HPA PRKD1: RNA low tissue specificity; no normal tissue stained high; highest cancer staining carcinoid (2 of 4 high). Distribution: 5 cancer families in the corpus carry a prevalence row, label threshold or catalogue link for it (Leukaemia, Myeloid neoplasms, Colorectal cancer, Prostate cancer, Biliary tract cancer (all types)); Open Targets associates it with 1 specific cancer type at or above 0.5 (acute myeloid leukemia). (Rule 6 of scripts/fetch-target-specificity.ts.)
Sources: UniProt Q15139; IntOGen PRKD1; Human Protein Atlas PRKD1 tissue; Open Targets ENSG00000184304 associations
First described 1994. Earliest sequence paper UniProt cites for the protein: Johannes F.-J. et al, J. Biol. Chem, 1994, "PKCmu is a novel, atypical member of the protein kinase C family". Source.
Sources: HGNC HGNC:9407 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt Q15139 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000184304 (association with cancer (MONDO_0004992) 0.68; per-cancer scores at or above 0.5: acute myeloid leukaemia 0.60, myeloproliferative neoplasm 0.60, systemic mastocytosis 0.54, leukaemia 0.64 (GraphQL API, CC0)); IntOGen PRKD1 (driver in 3 cohorts (Act 2, LoF 1); Compendium_Cancer_Genes.tsv release 20240920, CC0 1.0)
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 signalling, 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) signalling, 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. Location: Cytoplasm; Cell membrane; Golgi apparatus, trans-Golgi network (UniProt). Locus 14q12 (HGNC).
RNA: low tissue specificity, detected in many normal tissues.
No normal tissue stained high.
Medium only: cervical cancer, colorectal cancer, endometrial cancer, glioma.
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"PRKD1" OR ABSTRACT:"PRKD1" OR TITLE:"protein kinase D1" OR ABSTRACT:"protein kinase D1" OR TITLE:"Serine/threonine-protein kinase D1" OR ABSTRACT:"Serine/threonine-protein kinase D1" OR TITLE:"PKD1" OR ABSTRACT:"PKD1" OR TITLE:"PKC-mu" OR ABSTRACT:"PKC-mu" OR TITLE:"PRKCM" OR ABSTRACT:"PRKCM") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about PRKD1, not a curated reading list.
Shares Systemic mastocytosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis), Leukaemia (all types), Acute myeloid leukaemia.
Shares Systemic mastocytosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis), Leukaemia (all types), Acute myeloid leukaemia.
Shares Systemic mastocytosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis), Leukaemia (all types), Acute myeloid leukaemia.
Shares Systemic mastocytosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis), Leukaemia (all types), Acute myeloid leukaemia.
Shares Systemic mastocytosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis), Leukaemia (all types), Acute myeloid leukaemia.
Shares Systemic mastocytosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis), Leukaemia (all types), Acute myeloid leukaemia.
Shares Systemic mastocytosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis), Leukaemia (all types), Acute myeloid leukaemia.
Shares Systemic mastocytosis, Myeloproliferative neoplasms (PV, ET, myelofibrosis), Leukaemia (all types), Acute myeloid leukaemia.