PRKCI

Protein kinase C, iota

PDB rendering based on 1vd2.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1VD2, 1WMH, 1ZRZ, 3A8W, 3A8X, 3ZH8

Identifiers

Symbols

PRKCI ; DXS1179E; PKCI; nPKC-iota

External IDs

OMIM: 600539 MGI: 99260 HomoloGene: 37667 ChEMBL: 2598 GeneCards: PRKCI Gene

EC number

2.7.11.13

Gene ontology
Molecular function	• protein kinase activity • protein serine/threonine kinase activity • protein kinase C activity • protein binding • ATP binding • phospholipid binding • protein domain specific binding • metal ion binding
Cellular component	• Golgi membrane • nucleus • cytoplasm • endosome • cytosol • plasma membrane • bicellular tight junction • microtubule cytoskeleton • apical plasma membrane • cell leading edge • Schmidt-Lanterman incisure • protein complex • intercellular bridge • extracellular exosome
Biological process	• protein phosphorylation • protein targeting to membrane • cytoskeleton organization • actin filament organization • positive regulation of neuron projection development • vesicle-mediated transport • cell migration • cellular response to insulin stimulus • cell junction assembly • negative regulation of glial cell apoptotic process • establishment of apical/basal cell polarity • intracellular signal transduction • eye photoreceptor cell development • negative regulation of apoptotic process • negative regulation of neuron apoptotic process • establishment or maintenance of epithelial cell apical/basal polarity • cell-cell junction organization • positive regulation of glucose import • secretion • neurotrophin TRK receptor signaling pathway • Golgi vesicle budding • positive regulation of NF-kappaB transcription factor activity • positive regulation of glial cell proliferation • membrane organization • response to interleukin-1 • bicellular tight junction assembly • positive regulation of establishment of protein localization to plasma membrane • positive regulation of endothelial cell apoptotic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
170.22 – 170.31 Mb

Chr 3:
31 – 31.05 Mb

PubMed search

Protein kinase C iota type is an enzyme that in humans is encoded by the PRKCI gene.^[1]^[2]^[3]

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 phorbolesters 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.^[3]

Interactions

PRKCI has been shown to interact with:

Centaurin, alpha 1,^[4]
FRS2,^[5]
Glyceraldehyde 3-phosphate dehydrogenase,^[6]
PARD3,^[7]^[8]
Phosphoinositide-dependent kinase-1,^[9]
SMG1 (gene),^[10] and
Sequestosome 1.

References

↑ 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.
↑ 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.
1 2 "Entrez Gene: PRKCI protein kinase C, iota".
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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. PMC 230983. PMID 8524286.

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. PMID 2139676.
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. 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. doi:10.1038/333278a0. PMID 3259291.
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. 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. 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. 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.
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.

PDB gallery

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

1zrz: Crystal Structure of the Catalytic Domain of Atypical Protein Kinase C-iota

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

(3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(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)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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PRKCI

Function

Interactions

References

Further reading