PRKCI

Protein-coding gene in the species Homo sapiens
PRKCI
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1VD2, 1WMH, 1ZRZ, 3A8W, 3A8X, 3ZH8

Identifiers
AliasesPRKCI, DXS1179E, PKCI, nPKC-iota, protein kinase C iota
External IDsOMIM: 600539; MGI: 99260; HomoloGene: 37667; GeneCards: PRKCI; OMA:PRKCI - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for PRKCI
Genomic location for PRKCI
Band3q26.2Start170,222,424 bp[1]
End170,305,977 bp[1]
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)[2]
Chromosome 3 (mouse)
Genomic location for PRKCI
Genomic location for PRKCI
Band3 A3|3 14.65 cMStart31,049,896 bp[2]
End31,107,108 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • pylorus

  • lower lobe of lung

  • corpus epididymis

  • cardia

  • oral cavity

  • renal medulla

  • mucosa of pharynx

  • nipple

  • palpebral conjunctiva
Top expressed in
  • molar

  • ciliary body

  • urothelium

  • hair follicle

  • iris

  • conjunctival fornix

  • transitional epithelium of urinary bladder

  • epithelium of lens

  • primitive streak

  • ureter
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • protein kinase activity
  • nucleotide binding
  • protein kinase C activity
  • protein domain specific binding
  • metal ion binding
  • kinase activity
  • protein serine/threonine kinase activity
  • protein binding
  • phospholipid binding
  • ATP binding
Cellular component
  • cytosol
  • endosome
  • membrane
  • bicellular tight junction
  • microtubule cytoskeleton
  • Golgi membrane
  • plasma membrane
  • apical part of cell
  • Schmidt-Lanterman incisure
  • apical plasma membrane
  • cell leading edge
  • intercellular bridge
  • extracellular exosome
  • nucleus
  • cytoplasm
  • nucleoplasm
  • protein-containing complex
  • Schaffer collateral - CA1 synapse
  • glutamatergic synapse
Biological process
  • negative regulation of neuron apoptotic process
  • positive regulation of glucose import
  • establishment of apical/basal cell polarity
  • intracellular signal transduction
  • response to interleukin-1
  • phosphorylation
  • Golgi vesicle budding
  • actin filament organization
  • protein targeting to membrane
  • negative regulation of glial cell apoptotic process
  • response to peptide hormone
  • negative regulation of apoptotic process
  • secretion
  • protein phosphorylation
  • positive regulation of endothelial cell apoptotic process
  • positive regulation of NF-kappaB transcription factor activity
  • cytoskeleton organization
  • establishment or maintenance of epithelial cell apical/basal polarity
  • bicellular tight junction assembly
  • positive regulation of neuron projection development
  • cellular response to insulin stimulus
  • eye photoreceptor cell development
  • membrane organization
  • positive regulation of glial cell proliferation
  • cell migration
  • vesicle-mediated transport
  • cell-cell junction organization
  • peptidyl-serine phosphorylation
  • positive regulation of protein localization to plasma membrane
  • positive regulation of Notch signaling pathway
  • regulation of postsynaptic membrane neurotransmitter receptor levels
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5584

18759

Ensembl

ENSG00000163558

ENSMUSG00000037643

UniProt

P41743

Q62074

RefSeq (mRNA)

NM_002740

NM_008857

RefSeq (protein)

NP_002731

NP_032883

Location (UCSC)Chr 3: 170.22 – 170.31 MbChr 3: 31.05 – 31.11 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein kinase C iota type is an enzyme that in humans is encoded by the PRKCI gene.[5][6][7]

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.[7]

Interactions

PRKCI has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163558 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037643 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Mazzarella R, Ciccodicola A, Esposito T, Arcucci A, Migliaccio C, Jones C, Schlessinger D, D'Urso M, D'Esposito M (Apr 1995). "Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3". Genomics. 26 (3): 629–31. doi:10.1016/0888-7543(95)80190-W. PMID 7607695.
  6. ^ De Donato M, Gallagher DS, Davis SK, Stelly DM, Taylor JF (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. 95 (1–2): 79–81. doi:10.1159/000057021. PMID 11978974. S2CID 40052490.
  7. ^ a b "Entrez Gene: PRKCI protein kinase C, iota".
  8. ^ Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A (Aug 2003). "Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C". Biochemical and Biophysical Research Communications. 307 (3): 459–65. doi:10.1016/s0006-291x(03)01187-2. PMID 12893243.
  9. ^ Lim YP, Low BC, Lim J, Wong ES, Guy GR (Jul 1999). "Association of atypical protein kinase C isotypes with the docker protein FRS2 in fibroblast growth factor signaling". The Journal of Biological Chemistry. 274 (27): 19025–34. doi:10.1074/jbc.274.27.19025. PMID 10383403.
  10. ^ Tisdale EJ (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. 277 (5): 3334–41. doi:10.1074/jbc.M109744200. PMID 11724794.
  11. ^ Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT (May 1998). "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62". Molecular and Cellular Biology. 18 (5): 3069–80. doi:10.1128/mcb.18.5.3069. PMC 110686. PMID 9566925.
  12. ^ Kohjima M, Noda Y, Takeya R, Saito N, Takeuchi K, Sumimoto H (Dec 2002). "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes to tight junctions". Biochemical and Biophysical Research Communications. 299 (4): 641–6. doi:10.1016/s0006-291x(02)02698-0. PMID 12459187.
  13. ^ Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR (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. 275 (27): 20806–13. doi:10.1074/jbc.M000421200. PMID 10764742.
  14. ^ Diaz-Meco MT, Municio MM, Sanchez P, Lozano J, Moscat J (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. 16 (1): 105–14. doi:10.1128/mcb.16.1.105. PMC 230983. PMID 8524286.
  15. ^ Guo W, Wu S, Liu J, Fang B (Sep 2008). "Identification of a small molecule with synthetic lethality for K-ras and protein kinase C iota". Cancer Research. 68 (18): 7403–8. doi:10.1158/0008-5472.CAN-08-1449. PMC 2678915. PMID 18794128.
  16. ^ Ratnayake WS, Apostolatos AH, Ostrov DA, Acevedo-Duncan M (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. 51 (5): 1370–1382. doi:10.3892/ijo.2017.4131. PMC 5642393. PMID 29048609.
  17. ^ Ratnayake WS, Apostolatos CA, Apostolatos AH, Schutte RJ, Huynh MA, Ostrov DA, Acevedo-Duncan M (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. 12 (5): 1–17. doi:10.1080/19336918.2018.1471323. PMC 6363030. PMID 29781749.

Further reading

  • Suzuki A, Akimoto K, Ohno S (Jan 2003). "Protein kinase C lambda/iota (PKClambda/iota): a PKC isotype essential for the development of multicellular organisms". Journal of Biochemistry. 133 (1): 9–16. doi:10.1093/jb/mvg018. PMID 12761193.
  • Fields AP, Regala RP (Jun 2007). "Protein kinase C iota: human oncogene, prognostic marker and therapeutic target". Pharmacological Research. 55 (6): 487–97. doi:10.1016/j.phrs.2007.04.015. PMC 2705893. PMID 17570678.
  • Ruegg CL, Strand M (Oct 1991). "A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx". Cellular Immunology. 137 (1): 1–13. doi:10.1016/0008-8749(91)90051-C. PMID 1832084.
  • Chowdhury IH, Koyanagi Y, Kobayashi S, Hamamoto Y, Yoshiyama H, Yoshida T, Yamamoto N (May 1990). "The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway". Virology. 176 (1): 126–32. doi:10.1016/0042-6822(90)90237-L. PMID 1970444.
  • Ruegg CL, Strand M (May 1990). "Inhibition of protein kinase C and anti-CD3-induced Ca2+ influx in Jurkat T cells by a synthetic peptide with sequence identity to HIV-1 gp41". Journal of Immunology. 144 (10): 3928–35. doi:10.4049/jimmunol.144.10.3928. PMID 2139676. S2CID 44688726.
  • Jakobovits A, Rosenthal A, Capon DJ (Apr 1990). "Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C". The EMBO Journal. 9 (4): 1165–70. doi:10.1002/j.1460-2075.1990.tb08223.x. PMC 551792. PMID 2182321.
  • Fields AP, Bednarik DP, Hess A, May WS (May 1988). "Human immunodeficiency virus induces phosphorylation of its cell surface receptor". Nature. 333 (6170): 278–80. Bibcode:1988Natur.333..278F. doi:10.1038/333278a0. PMID 3259291. S2CID 4254146.
  • Chirmule N, Goonewardena H, Pahwa S, Pasieka R, Kalyanaraman VS, Pahwa S (Aug 1995). "HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells". The Journal of Biological Chemistry. 270 (33): 19364–9. doi:10.1074/jbc.270.33.19364. PMID 7642615.
  • Ward NE, Gravitt KR, O'Brian CA (Jan 1995). "Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein". Cancer Letters. 88 (1): 37–40. doi:10.1016/0304-3835(94)03610-U. PMID 7850771.
  • Gupta S, Aggarwal S, Kim C, Gollapudi S (Mar 1994). "Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report". International Journal of Immunopharmacology. 16 (3): 197–204. doi:10.1016/0192-0561(94)90013-2. PMID 8206685.
  • Selbie LA, Schmitz-Peiffer C, Sheng Y, Biden TJ (Nov 1993). "Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells". The Journal of Biological Chemistry. 268 (32): 24296–302. doi:10.1016/S0021-9258(20)80525-0. PMID 8226978.
  • Diaz-Meco MT, Municio MM, Sanchez P, Lozano J, Moscat J (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. 16 (1): 105–14. doi:10.1128/MCB.16.1.105. PMC 230983. PMID 8524286.
  • Parada NA, Cruikshank WW, Danis HL, Ryan TC, Center DM (Feb 1996). "IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C". Cellular Immunology. 168 (1): 100–6. doi:10.1006/cimm.1996.0054. PMID 8599832.
  • Conant K, Ma M, Nath A, Major EO (Mar 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". Journal of Virology. 70 (3): 1384–9. doi:10.1128/JVI.70.3.1384-1389.1996. PMC 189957. PMID 8627654.
  • Díaz-Meco MT, Municio MM, Frutos S, Sanchez P, Lozano J, Sanz L, Moscat J (Sep 1996). "The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C". Cell. 86 (5): 777–86. doi:10.1016/S0092-8674(00)80152-X. PMID 8797824. S2CID 15675524.
  • Holmes AM (Nov 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". Archives of Biochemistry and Biophysics. 335 (1): 8–12. doi:10.1006/abbi.1996.0476. PMID 8914829.
  • Murray NR, Fields AP (Oct 1997). "Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis". The Journal of Biological Chemistry. 272 (44): 27521–4. doi:10.1074/jbc.272.44.27521. PMID 9346882.
  • Borgatti P, Zauli G, Cantley LC, Capitani S (Jan 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". Biochemical and Biophysical Research Communications. 242 (2): 332–7. doi:10.1006/bbrc.1997.7877. PMID 9446795.
  • Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT (May 1998). "Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62". Molecular and Cellular Biology. 18 (5): 3069–80. doi:10.1128/mcb.18.5.3069. PMC 110686. PMID 9566925.
  • v
  • t
  • e
  • 1vd2: Solution Structure of the PB1 domain of PKCiota
    1vd2: Solution Structure of the PB1 domain of PKCiota
  • 1wmh: Crystal structure of a PB1 domain complex of Protein kinase c iota and Par6 alpha
    1wmh: Crystal structure of a PB1 domain complex of Protein kinase c iota and Par6 alpha
  • 1zrz: Crystal Structure of the Catalytic Domain of Atypical Protein Kinase C-iota
    1zrz: Crystal Structure of the Catalytic Domain of Atypical Protein Kinase C-iota
  • v
  • t
  • e
Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
  • -
IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(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)
MAP2K
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