PRKCI

Quality 0.50 · 3 views · Updated 2 months ago

Protein-coding gene in the species Homo sapiens

title: "PRKCI" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["ec-2.7.11"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/ec-2-7-11" source: "https://en.wikipedia.org/wiki/PRKCI" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Protein kinase C iota type is an enzyme that in humans is encoded by the PRKCI gene.

Function

This gene encodes a member of the protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbol esters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.

Interactions

PRKCI has been shown to interact with:

References

References

  1. (Apr 1995). "Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3". Genomics.
  2. (April 2002). "The assignment of PRKCI to bovine chromosome 1q34→q36 by FISH suggests a new assignment to human chromosome 3". Cytogenetics and Cell Genetics.
  3. "Entrez Gene: PRKCI protein kinase C, iota".
  4. (Aug 2003). "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C". Biochemical and Biophysical Research Communications.
  5. (Jul 1999). "Association of atypical protein kinase C isotypes with the docker protein FRS2 in fibroblast growth factor signaling". The Journal of Biological Chemistry.
  6. (Feb 2002). "Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway". The Journal of Biological Chemistry.
  7. (May 1998). "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62". Molecular and Cellular Biology.
  8. (Dec 2002). "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions". Biochemical and Biophysical Research Communications.
  9. (Jul 2000). "A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1". The Journal of Biological Chemistry.
  10. (Jan 1996). "Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo". Molecular and Cellular Biology.
  11. (Sep 2008). "Identification of a small molecule with synthetic lethality for K-ras and protein kinase C iota.". Cancer Research.
  12. (2017). "Two novel atypical PKC inhibitors; ACPD and DNDA effectively mitigate cell proliferation and epithelial to mesenchymal transition of metastatic melanoma while inducing apoptosis". Int. J. Oncol..
  13. (2018). "Oncogenic PKC-ι activates Vimentin during epithelial-mesenchymal transition in melanoma; a study based on PKC-ι and PKC-ζ specific inhibitors". Cell Adhes. Migr..

::callout[type=info title="Wikipedia Source"] This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page. ::

ec-2.7.11