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Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (PRKC-lambda/iota) (aPKC-lambda/iota) (nPKC-iota)

 KPCI_HUMAN              Reviewed;         596 AA.
P41743; D3DNQ4; Q8WW06;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
22-NOV-2017, entry version 200.
RecName: Full=Protein kinase C iota type;
EC=2.7.11.13;
AltName: Full=Atypical protein kinase C-lambda/iota;
Short=PRKC-lambda/iota;
Short=aPKC-lambda/iota;
AltName: Full=nPKC-iota;
Name=PRKCI; Synonyms=DXS1179E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=8226978;
Selbie L.A., Schmitz-Peiffer C., Sheng Y., Biden T.J.;
"Molecular cloning and characterization of PKC iota, an atypical
isoform of protein kinase C derived from insulin-secreting cells.";
J. Biol. Chem. 268:24296-24302(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Teratocarcinoma;
PubMed=7607695; DOI=10.1016/0888-7543(95)80190-W;
Mazzarella R., Ciccodicola A., Esposito T., Arcucci A., Migliaccio C.,
Jones C., Schlessinger D., D'Urso M., D'Esposito M.;
"Human protein kinase C iota gene (PRKCI) is closely linked to the BTK
gene in Xq21.3.";
Genomics 26:629-631(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH SMG1, AND ENZYME REGULATION.
PubMed=8524286; DOI=10.1128/MCB.16.1.105;
Diaz-Meco M.T., Municio M.M., Sanchez P., Lozano J., Moscat J.;
"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.";
Mol. Cell. Biol. 16:105-114(1996).
[6]
FUNCTION IN CELL SURVIVAL.
PubMed=9346882; DOI=10.1074/jbc.272.44.27521;
Murray N.R., Fields A.P.;
"Atypical protein kinase C iota protects human leukemia cells against
drug-induced apoptosis.";
J. Biol. Chem. 272:27521-27524(1997).
[7]
INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
PubMed=9566925; DOI=10.1128/MCB.18.5.3069;
Sanchez P., De Carcer G., Sandoval I.V., Moscat J., Diaz-Meco M.T.;
"Localization of atypical protein kinase C isoforms into lysosome-
targeted endosomes through interaction with p62.";
Mol. Cell. Biol. 18:3069-3080(1998).
[8]
FUNCTION IN CELL SURVIVAL.
PubMed=10467349; DOI=10.1038/sj.cdd.4400548;
Wooten M.W., Seibenhener M.L., Zhou G., Vandenplas M.L., Tan T.H.;
"Overexpression of atypical PKC in PC12 cells enhances NGF-
responsiveness and survival through an NF-kappaB dependent pathway.";
Cell Death Differ. 6:753-764(1999).
[9]
INTERACTION WITH SQSTM1 AND IKBKB, AND FUNCTION.
PubMed=10356400; DOI=10.1093/emboj/18.11.3044;
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.;
"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB
activation.";
EMBO J. 18:3044-3053(1999).
[10]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-274.
PubMed=10906326; DOI=10.1074/jbc.M002742200;
Spitaler M., Villunger A., Grunicke H., Uberall F.;
"Unique structural and functional properties of the ATP-binding domain
of atypical protein kinase C-iota.";
J. Biol. Chem. 275:33289-33296(2000).
[11]
FUNCTION IN CELL SURVIVAL.
PubMed=11042363; DOI=10.1016/S0169-328X(00)00187-X;
Xie J., Guo Q., Zhu H., Wooten M.W., Mattson M.P.;
"Protein kinase C iota protects neural cells against apoptosis induced
by amyloid beta-peptide.";
Brain Res. Mol. Brain Res. 82:107-113(2000).
[12]
INTERACTION WITH PARD6A; PARD6B AND PARD6G, AND SUBUNIT OF A COMPLEX
CONTAINING PARD6B AND CDC42/RAC1.
PubMed=11260256; DOI=10.1046/j.1365-2443.2001.00404.x;
Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.;
"Human homologues of the Caenorhabditis elegans cell polarity protein
PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to
atypical protein kinase C.";
Genes Cells 6:107-119(2001).
[13]
INTERACTION WITH PARD3 AND PARD6B IN THE TERNARY AKPC/PAR3/PAR6
COMPLEX.
PubMed=11257119; DOI=10.1083/jcb.152.6.1183;
Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M.,
Akimoto K., Izumi Y., Ohnishi T., Ohno S.;
"Atypical protein kinase C is involved in the evolutionarily conserved
par protein complex and plays a critical role in establishing
epithelia-specific junctional structures.";
J. Cell Biol. 152:1183-1196(2001).
[14]
FUNCTION, AND INTERACTION WITH GAPDH.
PubMed=11724794; DOI=10.1074/jbc.M109744200;
Tisdale E.J.;
"Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein
kinase Ciota /lambda and plays a role in microtubule dynamics in the
early secretory pathway.";
J. Biol. Chem. 277:3334-3341(2002).
[15]
PHOSPHORYLATION AT TYR-265; TYR-280 AND TYR-334, AND MUTAGENESIS OF
TYR-265; TYR-280 AND TYR-334.
PubMed=11713277; DOI=10.1128/MCB.21.24.8414-8427.2001;
Wooten M.W., Vandenplas M.L., Seibenhener M.L., Geetha T.,
Diaz-Meco M.T.;
"Nerve growth factor stimulates multisite tyrosine phosphorylation and
activation of the atypical protein kinase C's via a src kinase
pathway.";
Mol. Cell. Biol. 21:8414-8427(2001).
[16]
INTERACTION WITH KPNB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
TYR-265, AND MUTAGENESIS OF TYR-265.
PubMed=11891849; DOI=10.1002/jcb.10101.abs;
White W.O., Seibenhener M.L., Wooten M.W.;
"Phosphorylation of tyrosine 256 facilitates nuclear import of
atypical protein kinase C.";
J. Cell. Biochem. 85:42-53(2002).
[17]
INTERACTION WITH ADAP1.
PubMed=12893243; DOI=10.1016/S0006-291X(03)01187-2;
Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D.,
Wakefield R.I.D., Johannes F.-J., Aitken A.;
"Centaurin-alpha(1) associates with and is phosphorylated by isoforms
of protein kinase C.";
Biochem. Biophys. Res. Commun. 307:459-465(2003).
[18]
INTERACTION WITH PARD6B/PAR-6 AND LLGL1.
PubMed=12725730; DOI=10.1016/S0960-9822(03)00244-6;
Yamanaka T., Horikoshi Y., Sugiyama Y., Ishiyama C., Suzuki A.,
Hirose T., Iwamatsu A., Shinohara A., Ohno S.;
"Mammalian Lgl forms a protein complex with PAR-6 and aPKC
independently of PAR-3 to regulate epithelial cell polarity.";
Curr. Biol. 13:734-743(2003).
[19]
FUNCTION.
PubMed=12871960; DOI=10.1074/jbc.M305381200;
Tisdale E.J., Wang J., Silver R.B., Artalejo C.R.;
"Atypical protein kinase C plays a critical role in protein transport
from pre-Golgi intermediates.";
J. Biol. Chem. 278:38015-38021(2003).
[20]
INTERACTION WITH RAB2A.
PubMed=14570876; DOI=10.1074/jbc.M309343200;
Tisdale E.J.;
"Rab2 interacts directly with atypical protein kinase C (aPKC)
iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-
phosphate dehydrogenase phosphorylation.";
J. Biol. Chem. 278:52524-52530(2003).
[21]
FUNCTION IN PHOSPHORYLATION OF IRAK1.
PubMed=14684752; DOI=10.1074/jbc.C300431200;
Mamidipudi V., Lin C., Seibenhener M.L., Wooten M.W.;
"Regulation of interleukin receptor-associated kinase (IRAK)
phosphorylation and signaling by iota protein kinase C.";
J. Biol. Chem. 279:4161-4165(2004).
[22]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15994303; DOI=10.1074/jbc.M505402200;
Regala R.P., Weems C., Jamieson L., Copland J.A., Thompson E.A.,
Fields A.P.;
"Atypical protein kinase Ciota plays a critical role in human lung
cancer cell growth and tumorigenicity.";
J. Biol. Chem. 280:31109-31115(2005).
[23]
INTERACTION WITH CDK7, AND SUBCELLULAR LOCATION.
PubMed=15695176; DOI=10.1016/j.tice.2004.10.004;
Bicaku E., Patel R., Acevedo-Duncan M.;
"Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-
iota in human glioma cells.";
Tissue Cell 37:53-58(2005).
[24]
INTERACTION WITH WDFY2.
PubMed=16792529; DOI=10.1042/BJ20060511;
Fritzius T., Burkard G., Haas E., Heinrich J., Schweneker M.,
Bosse M., Zimmermann S., Frey A.D., Caelers A., Bachmann A.S.,
Moelling K.;
"A WD-FYVE protein binds to the kinases Akt and PKCzeta/lambda.";
Biochem. J. 399:9-20(2006).
[25]
INTERACTION WITH RAB2A AND GADPH, PHOSPHORYLATION, AND SUBCELLULAR
LOCATION.
PubMed=16452474; DOI=10.1074/jbc.M513031200;
Tisdale E.J., Artalejo C.R.;
"Src-dependent protein kinase C iota/lambda (aPKCiota/lambda) tyrosine
phosphorylation is required for aPKCiota/lambda association with Rab2
and glyceraldehyde-3-phosphate dehydrogenase on pre-Golgi
intermediates.";
J. Biol. Chem. 281:8436-8442(2006).
[26]
INTERACTION WITH VAMP2.
PubMed=17313651; DOI=10.1111/j.1742-4658.2007.05702.x;
Fritzius T., Frey A.D., Schweneker M., Mayer D., Moelling K.;
"WD-repeat-propeller-FYVE protein, ProF, binds VAMP2 and protein
kinase Czeta.";
FEBS J. 274:1552-1566(2007).
[27]
FUNCTION IN PHOSPHORYLATION OF EZR.
PubMed=18270268; DOI=10.1242/jcs.016246;
Wald F.A., Oriolo A.S., Mashukova A., Fregien N.L., Langshaw A.H.,
Salas P.J.;
"Atypical protein kinase C (iota) activates ezrin in the apical domain
of intestinal epithelial cells.";
J. Cell Sci. 121:644-654(2008).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[31]
FUNCTION IN APOPTOSIS.
PubMed=19327373; DOI=10.1016/j.mvr.2009.01.014;
Staiger K., Schatz U., Staiger H., Weyrich P., Haas C., Guirguis A.,
Machicao F., Haering H.U., Kellerer M.;
"Protein kinase C iota mediates lipid-induced apoptosis of human
coronary artery endothelial cells.";
Microvasc. Res. 78:40-44(2009).
[32]
INTERACTION WITH ECT2 AND PARD6A, AND MUTAGENESIS OF ASP-72.
PubMed=19617897; DOI=10.1038/onc.2009.217;
Justilien V., Fields A.P.;
"Ect2 links the PKCiota-Par6alpha complex to Rac1 activation and
cellular transformation.";
Oncogene 28:3597-3607(2009).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT PRO-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT THR-3; SER-7; SER-8 AND THR-9, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[36]
FUNCTION IN PHOSPHORYLATION OF BAD.
PubMed=21419810; DOI=10.1016/j.bbamcr.2011.03.007;
Desai S., Pillai P., Win-Piazza H., Acevedo-Duncan M.;
"PKC-? promotes glioblastoma cell survival by phosphorylating and
inhibiting BAD through a phosphatidylinositol 3-kinase pathway.";
Biochim. Biophys. Acta 1813:1190-1197(2011).
[37]
FUNCTION IN PHOSPHORYLATION OF ECT2.
PubMed=21189248; DOI=10.1074/jbc.M110.196113;
Justilien V., Jameison L., Der C.J., Rossman K.L., Fields A.P.;
"Oncogenic activity of Ect2 is regulated through protein kinase C
iota-mediated phosphorylation.";
J. Biol. Chem. 286:8149-8157(2011).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[41]
STRUCTURE BY NMR OF 25-108, INTERACTION WITH SQSTM1 AND MAP2K5, AND
MUTAGENESIS OF LYS-29 AND ASP-72.
PubMed=15143057; DOI=10.1074/jbc.M403092200;
Hirano Y., Yoshinaga S., Ogura K., Yokochi M., Noda Y., Sumimoto H.,
Inagaki F.;
"Solution structure of atypical protein kinase C PB1 domain and its
mode of interaction with ZIP/p62 and MEK5.";
J. Biol. Chem. 279:31883-31890(2004).
[42]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-108 IN COMPLEX WITH
PARD6A, AND MUTAGENESIS OF ASP-72; GLU-85 AND ARG-91.
PubMed=15590654; DOI=10.1074/jbc.M409823200;
Hirano Y., Yoshinaga S., Takeya R., Suzuki N.N., Horiuchi M.,
Kohjima M., Sumimoto H., Inagaki F.;
"Structure of a cell polarity regulator, a complex between atypical
PKC and Par6 PB1 domains.";
J. Biol. Chem. 280:9653-9661(2005).
[43]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-596, IDENTIFICATION BY
MASS SPECTROMETRY, AND PHOSPHORYLATION AT THR-412 AND THR-564.
PubMed=16125198; DOI=10.1016/j.jmb.2005.07.060;
Messerschmidt A., Macieira S., Velarde M., Baedeker M., Benda C.,
Jestel A., Brandstetter H., Neuefeind T., Blaesse M.;
"Crystal structure of the catalytic domain of human atypical protein
kinase C-iota reveals interaction mode of phosphorylation site in turn
motif.";
J. Mol. Biol. 352:918-931(2005).
[44]
VARIANTS [LARGE SCALE ANALYSIS] LEU-118 AND CYS-130.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Calcium- and diacylglycerol-independent serine/
threonine-protein kinase that plays a general protective role
against apoptotic stimuli, is involved in NF-kappa-B activation,
cell survival, differentiation and polarity, and contributes to
the regulation of microtubule dynamics in the early secretory
pathway. Is necessary for BCR-ABL oncogene-mediated resistance to
apoptotic drug in leukemia cells, protecting leukemia cells
against drug-induced apoptosis. In cultured neurons, prevents
amyloid beta protein-induced apoptosis by interrupting cell death
process at a very early step. In glioblastoma cells, may function
downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in
the promotion of cell survival by phosphorylating and inhibiting
the pro-apoptotic factor BAD. Can form a protein complex in non-
small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and
regulate ECT2 oncogenic activity by phosphorylation, which in turn
promotes transformed growth and invasion. In response to nerve
growth factor (NGF), acts downstream of SRC to phosphorylate and
activate IRAK1, allowing the subsequent activation of NF-kappa-B
and neuronal cell survival. Functions in the organization of the
apical domain in epithelial cells by phosphorylating EZR. This
step is crucial for activation and normal distribution of EZR at
the early stages of intestinal epithelial cell differentiation.
Forms a protein complex with LLGL1 and PARD6B independently of
PARD3 to regulate epithelial cell polarity. Plays a role in
microtubule dynamics in the early secretory pathway through
interaction with RAB2A and GAPDH and recruitment to vesicular
tubular clusters (VTCs). In human coronary artery endothelial
cells (HCAEC), is activated by saturated fatty acids and mediates
lipid-induced apoptosis. {ECO:0000269|PubMed:10356400,
ECO:0000269|PubMed:10467349, ECO:0000269|PubMed:10906326,
ECO:0000269|PubMed:11042363, ECO:0000269|PubMed:11724794,
ECO:0000269|PubMed:12871960, ECO:0000269|PubMed:14684752,
ECO:0000269|PubMed:15994303, ECO:0000269|PubMed:18270268,
ECO:0000269|PubMed:19327373, ECO:0000269|PubMed:21189248,
ECO:0000269|PubMed:21419810, ECO:0000269|PubMed:8226978,
ECO:0000269|PubMed:9346882}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Atypical PKCs (PRKCI and PRKCZ) exhibit an
elevated basal enzymatic activity (that may be due to the
interaction with SMG1 or SQSTM1) and are not regulated by
diacylglycerol, phosphatidylserine, phorbol esters or calcium
ions. Two specific sites, Thr-412 (activation loop of the kinase
domain) and Thr-564 (turn motif), need to be phosphorylated for
its full activation (By similarity). Might also be a target for
novel lipid activators that are elevated during nutrient-
stimulated insulin secretion. {ECO:0000250,
ECO:0000269|PubMed:8524286}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=13.5 uM for ATP (for recombinant purified PRKCI)
{ECO:0000269|PubMed:10906326};
Vmax=7.4 pmol/min/mg enzyme {ECO:0000269|PubMed:10906326};
-!- SUBUNIT: Forms a complex with SQSTM1 and MP2K5 (By similarity).
Interacts directly with SQSTM1 (Probable). Interacts with IKBKB.
Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary
complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or
PARD6G) and a GTPase protein (CDC42 or RAC1). Part of a complex
with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction
with SMG1, through the ZN-finger domain, activates the kinase
activity. Interacts with CDK7. Forms a complex with RAB2A and
GAPDH involved in recruitment onto the membrane of vesicular
tubular clusters (VTCs). Interacts with ECT2 ('Thr-359'
phosphorylated form). Interacts with VAMP2 (PubMed:17313651).
Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529).
{ECO:0000250|UniProtKB:Q62074, ECO:0000269|PubMed:10356400,
ECO:0000269|PubMed:11257119, ECO:0000269|PubMed:11260256,
ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:11891849,
ECO:0000269|PubMed:12725730, ECO:0000269|PubMed:12893243,
ECO:0000269|PubMed:14570876, ECO:0000269|PubMed:15143057,
ECO:0000269|PubMed:15590654, ECO:0000269|PubMed:15695176,
ECO:0000269|PubMed:16452474, ECO:0000269|PubMed:16792529,
ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:19617897,
ECO:0000269|PubMed:8524286, ECO:0000269|PubMed:9566925,
ECO:0000305}.
-!- INTERACTION:
P60953:CDC42; NbExp=5; IntAct=EBI-286199, EBI-81752;
P78545:ELF3; NbExp=2; IntAct=EBI-286199, EBI-1057285;
P08151-1:GLI1; NbExp=3; IntAct=EBI-286199, EBI-16038799;
Q96L34:MARK4; NbExp=2; IntAct=EBI-286199, EBI-302319;
Q8TEW0:PARD3; NbExp=3; IntAct=EBI-286199, EBI-81968;
Q9NPB6:PARD6A; NbExp=12; IntAct=EBI-286199, EBI-81876;
Q9NPB6-2:PARD6A; NbExp=4; IntAct=EBI-286199, EBI-10693102;
Q9BYG5:PARD6B; NbExp=15; IntAct=EBI-286199, EBI-295391;
Q9BYG4:PARD6G; NbExp=5; IntAct=EBI-286199, EBI-295417;
Q8ND90:PNMA1; NbExp=2; IntAct=EBI-286199, EBI-302345;
Q05513:PRKCZ; NbExp=4; IntAct=EBI-286199, EBI-295351;
P63000:RAC1; NbExp=3; IntAct=EBI-286199, EBI-413628;
P48431:SOX2; NbExp=2; IntAct=EBI-286199, EBI-6124081;
Q13501:SQSTM1; NbExp=7; IntAct=EBI-286199, EBI-307104;
Q04917:YWHAH; NbExp=3; IntAct=EBI-286199, EBI-306940;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11891849,
ECO:0000269|PubMed:15695176, ECO:0000269|PubMed:9566925}. Membrane
{ECO:0000269|PubMed:16452474}. Endosome
{ECO:0000269|PubMed:9566925}. Nucleus
{ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:15695176}.
Note=Transported into the endosome through interaction with
SQSTM1/p62. After phosphorylation by SRC, transported into the
nucleus through interaction with KPNB1. Colocalizes with CDK7 in
the cytoplasm and nucleus. Transported to vesicular tubular
clusters (VTCs) through interaction with RAB2A.
{ECO:0000269|PubMed:15695176, ECO:0000269|PubMed:9566925}.
-!- TISSUE SPECIFICITY: Predominantly expressed in lung and brain, but
also expressed at lower levels in many tissues including
pancreatic islets. Highly expressed in non-small cell lung
cancers. {ECO:0000269|PubMed:15994303, ECO:0000269|PubMed:7607695,
ECO:0000269|PubMed:8226978}.
-!- DOMAIN: The PB1 domain mediates interaction with SQSTM1.
{ECO:0000250}.
-!- DOMAIN: The C1 zinc finger does not bind diacylglycerol (DAG).
-!- DOMAIN: The pseudosubstrate motif resembles the sequence around
sites phosphorylated on target proteins, except the presence of a
non-phosphorylatable residue in place of Ser, it modulates
activity by competing with substrates. {ECO:0000250}.
-!- PTM: Phosphorylation at Thr-412 in the activation loop is not
mandatory for activation (By similarity). Upon neuronal growth
factor (NGF) stimulation, phosphorylated by SRC at Tyr-265, Tyr-
280 and Tyr-334. Phosphorylation at Tyr-265 facilitates binding to
KPNB1/importin-beta regulating entry of PRKCI into the nucleus.
Phosphorylation on Tyr-334 is important for NF-kappa-B
stimulation. {ECO:0000250, ECO:0000269|PubMed:11713277,
ECO:0000269|PubMed:11891849, ECO:0000269|PubMed:16125198,
ECO:0000269|PubMed:16452474}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA60171.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAB17011.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH22016.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PRKCIID41857ch3q26.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L18964; AAA60171.1; ALT_INIT; mRNA.
EMBL; L33881; AAB17011.1; ALT_INIT; mRNA.
EMBL; CH471052; EAW78513.1; -; Genomic_DNA.
EMBL; CH471052; EAW78515.1; -; Genomic_DNA.
EMBL; BC022016; AAH22016.3; ALT_INIT; mRNA.
CCDS; CCDS3212.2; -.
PIR; A49509; A49509.
RefSeq; NP_002731.4; NM_002740.5.
UniGene; Hs.478199; -.
PDB; 1VD2; NMR; -; A=25-108.
PDB; 1WMH; X-ray; 1.50 A; A=25-108.
PDB; 1ZRZ; X-ray; 3.00 A; A=233-596.
PDB; 3A8W; X-ray; 2.10 A; A/B=249-588.
PDB; 3A8X; X-ray; 2.00 A; A/B=249-588.
PDB; 3ZH8; X-ray; 2.74 A; A/B/C=248-594.
PDB; 5LI1; X-ray; 2.00 A; A=248-596.
PDB; 5LI9; X-ray; 1.79 A; A=248-596.
PDB; 5LIH; X-ray; 3.25 A; A/B=248-596.
PDBsum; 1VD2; -.
PDBsum; 1WMH; -.
PDBsum; 1ZRZ; -.
PDBsum; 3A8W; -.
PDBsum; 3A8X; -.
PDBsum; 3ZH8; -.
PDBsum; 5LI1; -.
PDBsum; 5LI9; -.
PDBsum; 5LIH; -.
ProteinModelPortal; P41743; -.
SMR; P41743; -.
BioGrid; 111570; 89.
CORUM; P41743; -.
DIP; DIP-31311N; -.
ELM; P41743; -.
IntAct; P41743; 56.
MINT; MINT-5004219; -.
STRING; 9606.ENSP00000295797; -.
BindingDB; P41743; -.
ChEMBL; CHEMBL2598; -.
DrugBank; DB03777; Rbt205 Inhibitor.
DrugBank; DB00675; Tamoxifen.
GuidetoPHARMACOLOGY; 1490; -.
iPTMnet; P41743; -.
PhosphoSitePlus; P41743; -.
BioMuta; PRKCI; -.
DMDM; 239938658; -.
EPD; P41743; -.
MaxQB; P41743; -.
PaxDb; P41743; -.
PeptideAtlas; P41743; -.
PRIDE; P41743; -.
DNASU; 5584; -.
Ensembl; ENST00000295797; ENSP00000295797; ENSG00000163558.
GeneID; 5584; -.
KEGG; hsa:5584; -.
UCSC; uc003fgs.3; human.
CTD; 5584; -.
DisGeNET; 5584; -.
EuPathDB; HostDB:ENSG00000163558.12; -.
GeneCards; PRKCI; -.
HGNC; HGNC:9404; PRKCI.
HPA; HPA026574; -.
HPA; HPA038635; -.
MIM; 600539; gene.
neXtProt; NX_P41743; -.
OpenTargets; ENSG00000163558; -.
PharmGKB; PA33768; -.
eggNOG; KOG0695; Eukaryota.
eggNOG; ENOG410ZMG2; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P41743; -.
KO; K06069; -.
OMA; KGDIMIT; -.
OrthoDB; EOG091G03Q9; -.
PhylomeDB; P41743; -.
TreeFam; TF102004; -.
BRENDA; 2.7.11.13; 2681.
Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
Reactome; R-HSA-420029; Tight junction interactions.
SABIO-RK; P41743; -.
SignaLink; P41743; -.
SIGNOR; P41743; -.
ChiTaRS; PRKCI; human.
EvolutionaryTrace; P41743; -.
GeneWiki; PRKCI; -.
GenomeRNAi; 5584; -.
PRO; PR:P41743; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163558; -.
CleanEx; HS_PRKCI; -.
Genevisible; P41743; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004697; F:protein kinase C activity; ISS:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0070830; P:bicellular tight junction assembly; TAS:Reactome.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0045216; P:cell-cell junction organization; IMP:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
GO; GO:0035089; P:establishment of apical/basal cell polarity; IEA:Ensembl.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; TAS:UniProtKB.
GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
GO; GO:0048194; P:Golgi vesicle budding; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; NAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IMP:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IMP:UniProtKB.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; ISS:BHF-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0006612; P:protein targeting to membrane; NAS:UniProtKB.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
GO; GO:0046903; P:secretion; NAS:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB.
CDD; cd00029; C1; 1.
CDD; cd06404; PB1_aPKC; 1.
CDD; cd05618; STKc_aPKC_iota; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034661; aPKC_iota.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR034877; PB1_aPKC.
InterPro; IPR000270; PB1_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR012233; PKC.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 1.
Pfam; PF00564; PB1; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000554; PKC_zeta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00666; PB1; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS51745; PB1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Endosome; Kinase; Membrane; Metal-binding; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Tumor suppressor; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231}.
CHAIN 2 596 Protein kinase C iota type.
/FTId=PRO_0000055710.
DOMAIN 25 108 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 254 522 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 523 594 AGC-kinase C-terminal.
ZN_FING 140 190 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 260 268 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 253 Regulatory domain.
REGION 2 28 Required for interaction with RAB2.
REGION 72 91 Interaction with PARD6A.
MOTIF 125 134 Pseudosubstrate. {ECO:0000250}.
ACT_SITE 378 378 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 283 283 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylproline.
{ECO:0000244|PubMed:20068231}.
MOD_RES 3 3 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 265 265 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:11713277,
ECO:0000269|PubMed:11891849}.
MOD_RES 280 280 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:11713277}.
MOD_RES 334 334 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:11713277}.
MOD_RES 412 412 Phosphothreonine; by PDPK1.
{ECO:0000305|PubMed:16125198}.
MOD_RES 564 564 Phosphothreonine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16125198}.
VARIANT 118 118 P -> L (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042322.
VARIANT 130 130 R -> C (in dbSNP:rs56154494).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042323.
MUTAGEN 29 29 K->A: No effect on interaction with
SQSTM1. {ECO:0000269|PubMed:15143057}.
MUTAGEN 72 72 D->A: Loss of interaction with ECT2,
PARD6A and with SQSTM1.
{ECO:0000269|PubMed:15143057,
ECO:0000269|PubMed:15590654,
ECO:0000269|PubMed:19617897}.
MUTAGEN 85 85 E->A: Slight decrease of interaction with
PARD6A. Loss of interaction with PARD6A;
when associated with A-91.
{ECO:0000269|PubMed:15590654}.
MUTAGEN 91 91 R->A: Slight decrease of interaction with
PARD6A. Loss of interaction with PARD6A;
when associated with A-85.
{ECO:0000269|PubMed:15590654}.
MUTAGEN 265 265 Y->F: No effect on the SRC-mediated
phosphorylation state. No effect on SRC-
induced enzyme activity. Little effect on
TRAF6-mediated activation of NF-kappa-B.
Decreased binding to KPNB1/importin-beta.
{ECO:0000269|PubMed:11713277,
ECO:0000269|PubMed:11891849}.
MUTAGEN 274 274 K->R: No effect on activity.
{ECO:0000269|PubMed:10906326}.
MUTAGEN 274 274 K->W: Abolishes activity.
{ECO:0000269|PubMed:10906326}.
MUTAGEN 280 280 Y->F: No effect on the SRC-mediated
phosphorylation state. No effect on SRC-
induced enzyme activity. No effect on
TRAF6-mediated activation of NF-kappa-B.
{ECO:0000269|PubMed:11713277}.
MUTAGEN 334 334 Y->F: No effect on the SRC-mediated
phosphorylation state. Significant
reduction of SRC-induced enzyme activity.
Greatly reduced TRAF6-mediated activation
of NF-kappa-B. Reduces NGF-dependent cell
survival. {ECO:0000269|PubMed:11713277}.
CONFLICT 485 485 L -> M (in Ref. 4; AAH22016).
{ECO:0000305}.
CONFLICT 508 508 H -> L (in Ref. 4; AAH22016).
{ECO:0000305}.
CONFLICT 560 560 P -> R (in Ref. 4; AAH22016).
{ECO:0000305}.
STRAND 26 32 {ECO:0000244|PDB:1WMH}.
STRAND 35 41 {ECO:0000244|PDB:1WMH}.
HELIX 47 57 {ECO:0000244|PDB:1WMH}.
STRAND 67 71 {ECO:0000244|PDB:1WMH}.
STRAND 73 75 {ECO:0000244|PDB:1VD2}.
STRAND 77 79 {ECO:0000244|PDB:1WMH}.
HELIX 83 95 {ECO:0000244|PDB:1WMH}.
STRAND 101 106 {ECO:0000244|PDB:1WMH}.
HELIX 251 253 {ECO:0000244|PDB:5LI9}.
STRAND 254 262 {ECO:0000244|PDB:5LI9}.
STRAND 264 273 {ECO:0000244|PDB:5LI9}.
TURN 274 277 {ECO:0000244|PDB:3A8X}.
STRAND 279 286 {ECO:0000244|PDB:5LI9}.
HELIX 287 289 {ECO:0000244|PDB:5LI9}.
HELIX 293 309 {ECO:0000244|PDB:5LI9}.
STRAND 318 323 {ECO:0000244|PDB:5LI9}.
STRAND 325 332 {ECO:0000244|PDB:5LI9}.
HELIX 340 347 {ECO:0000244|PDB:5LI9}.
HELIX 352 371 {ECO:0000244|PDB:5LI9}.
HELIX 381 383 {ECO:0000244|PDB:5LI9}.
STRAND 384 386 {ECO:0000244|PDB:5LI9}.
STRAND 388 390 {ECO:0000244|PDB:3ZH8}.
STRAND 392 394 {ECO:0000244|PDB:5LI9}.
HELIX 397 399 {ECO:0000244|PDB:3A8X}.
HELIX 417 419 {ECO:0000244|PDB:5LI9}.
HELIX 422 425 {ECO:0000244|PDB:5LI9}.
HELIX 433 448 {ECO:0000244|PDB:5LI9}.
TURN 452 457 {ECO:0000244|PDB:3A8X}.
HELIX 467 476 {ECO:0000244|PDB:5LI9}.
HELIX 487 496 {ECO:0000244|PDB:5LI9}.
TURN 501 503 {ECO:0000244|PDB:5LI9}.
TURN 505 507 {ECO:0000244|PDB:1ZRZ}.
TURN 509 511 {ECO:0000244|PDB:5LI9}.
HELIX 512 517 {ECO:0000244|PDB:5LI9}.
HELIX 520 522 {ECO:0000244|PDB:5LI9}.
HELIX 527 531 {ECO:0000244|PDB:5LI9}.
TURN 545 547 {ECO:0000244|PDB:5LI9}.
HELIX 549 551 {ECO:0000244|PDB:3A8X}.
HELIX 554 557 {ECO:0000244|PDB:5LI9}.
HELIX 568 571 {ECO:0000244|PDB:5LI9}.
HELIX 576 579 {ECO:0000244|PDB:5LI9}.
SEQUENCE 596 AA; 68262 MW; 1E3F8C1D4BFC734F CRC64;
MPTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CNEVRDMCSF
DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE
DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK
KCHKLVTIEC GRHSLPQEPV MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR
ESGKASSSLG LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ
TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA
EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI
APEILRGEDY GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR
IPRSLSVKAA SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK
PNISGEFGLD NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV


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CSB-EL018707HU Human Protein kinase C iota type(PRKCI) ELISA kit 96T
G3510 Protein kinase C iota type (PRKCI), Mouse, ELISA Kit 96T
G3509 Protein kinase C iota type (PRKCI), Human, ELISA Kit 96T
CSB-EL018707MO Mouse Protein kinase C iota type(PRKCI) ELISA kit 96T
CSB-EL018707HU Human Protein kinase C iota type(PRKCI) ELISA kit SpeciesHuman 96T
CSB-EL018707MO Mouse Protein kinase C iota type(PRKCI) ELISA kit SpeciesMouse 96T
E02P0106 Rat Protein Kinase C Iota ELISA 96T/kit
KPCI_HUMAN ELISA Kit FOR Protein kinase C iota type; organism: Human; gene name: PRKCI 96T


 

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