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Protein kinase C eta type (EC 2.7.11.13) (PKC-L) (nPKC-eta)

 KPCL_HUMAN              Reviewed;         683 AA.
P24723; B4DJN5; Q16246; Q8NE03;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
15-DEC-2009, sequence version 4.
25-OCT-2017, entry version 187.
RecName: Full=Protein kinase C eta type;
EC=2.7.11.13;
AltName: Full=PKC-L;
AltName: Full=nPKC-eta;
Name=PRKCH; Synonyms=PKCL, PRKCL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Lung;
PubMed=1986216; DOI=10.1128/MCB.11.1.126;
Bacher N., Zisman Y., Berent E., Livneh E.;
"Isolation and characterization of PKC-L, a new member of the protein
kinase C-related gene family specifically expressed in lung, skin, and
heart.";
Mol. Cell. Biol. 11:126-133(1991).
[2]
ERRATUM, AND SEQUENCE REVISION.
PubMed=1545821;
Bacher N., Zisman Y., Berent E., Livneh E.;
Mol. Cell. Biol. 12:1404-1404(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 438-539 (ISOFORM 1).
PubMed=7988719; DOI=10.1016/0014-5793(94)01202-4;
Palmer R.H., Ridden J., Parker P.J.;
"Identification of multiple, novel, protein kinase C-related gene
products.";
FEBS Lett. 356:5-8(1994).
[8]
FUNCTION.
PubMed=11112424; DOI=10.1006/bbrc.2000.3903;
Akkaraju G.R., Basu A.;
"Overexpression of protein kinase C-eta attenuates caspase activation
and tumor necrosis factor-alpha-induced cell death.";
Biochem. Biophys. Res. Commun. 279:103-107(2000).
[9]
FUNCTION IN CELL PROLIFERATION.
PubMed=10806212; DOI=10.1074/jbc.M003203200;
Hussaini I.M., Karns L.R., Vinton G., Carpenter J.E., Redpath G.T.,
Sando J.J., VandenBerg S.R.;
"Phorbol 12-myristate 13-acetate induces protein kinase ceta-specific
proliferative response in astrocytic tumor cells.";
J. Biol. Chem. 275:22348-22354(2000).
[10]
FUNCTION.
PubMed=11772428; DOI=10.1093/neuonc/4.1.9;
Hussaini I.M., Carpenter J.E., Redpath G.T., Sando J.J.,
Shaffrey M.E., Vandenberg S.R.;
"Protein kinase C-eta regulates resistance to UV- and gamma-
irradiation-induced apoptosis in glioblastoma cells by preventing
caspase-9 activation.";
Neuro-oncol. 4:9-21(2002).
[11]
FUNCTION IN CELL PROLIFERATION.
PubMed=15489897; DOI=10.1038/sj.onc.1208093;
Aeder S.E., Martin P.M., Soh J.W., Hussaini I.M.;
"PKC-eta mediates glioblastoma cell proliferation through the Akt and
mTOR signaling pathways.";
Oncogene 23:9062-9069(2004).
[12]
INTERACTION WITH DGKQ.
PubMed=15632189; DOI=10.1074/jbc.M409301200;
van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.;
"Translocation of diacylglycerol kinase theta from cytosol to plasma
membrane in response to activation of G protein-coupled receptors and
protein kinase C.";
J. Biol. Chem. 280:9870-9878(2005).
[13]
FUNCTION.
PubMed=17146445; DOI=10.1038/sj.onc.1210090;
Uht R.M., Amos S., Martin P.M., Riggan A.E., Hussaini I.M.;
"The protein kinase C-eta isoform induces proliferation in
glioblastoma cell lines through an ERK/Elk-1 pathway.";
Oncogene 26:2885-2893(2007).
[14]
FUNCTION IN B-CELL SIGNALING.
PubMed=18780722; DOI=10.1093/intimm/dxn101;
Oda A., Ono T., Yamamoto M., Goitsuka R., Kitamura D.;
"PKC eta directs induction of IRF-4 expression and Ig kappa gene
rearrangement in pre-BCR signaling pathway.";
Int. Immunol. 20:1417-1426(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
FUNCTION IN PHOSPHORYLATION OF OCLN.
PubMed=19114660; DOI=10.1073/pnas.0802741106;
Suzuki T., Elias B.C., Seth A., Shen L., Turner J.R., Giorgianni F.,
Desiderio D., Guntaka R., Rao R.;
"PKC eta regulates occludin phosphorylation and epithelial tight
junction integrity.";
Proc. Natl. Acad. Sci. U.S.A. 106:61-66(2009).
[17]
FUNCTION.
PubMed=20558593; DOI=10.1124/mol.110.064394;
Lee H.K., Yeo S., Kim J.S., Lee J.G., Bae Y.S., Lee C., Baek S.H.;
"Protein kinase C-eta and phospholipase D2 pathway regulates foam cell
formation via regulator of G protein signaling 2.";
Mol. Pharmacol. 78:478-485(2010).
[18]
FUNCTION.
PubMed=21820409; DOI=10.1016/j.bbrc.2011.07.090;
Raveh-Amit H., Hai N., Rotem-Dai N., Shahaf G., Gopas J., Livneh E.;
"Protein kinase C? activates NF-?B in response to camptothecin-induced
DNA damage.";
Biochem. Biophys. Res. Commun. 412:313-317(2011).
[19]
REVIEW.
PubMed=12473186; DOI=10.1093/oxfordjournals.jbchem.a003297;
Kashiwagi M., Ohba M., Chida K., Kuroki T.;
"Protein kinase C eta (PKC eta): its involvement in keratinocyte
differentiation.";
J. Biochem. 132:853-857(2002).
[20]
FUNCTION.
PubMed=22304920; DOI=10.1016/j.cell.2012.01.016;
Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L.,
Ideker T., Ronai Z.A.;
"PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while
blocking its apoptotic function at mitochondria.";
Cell 148:543-555(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-656, 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).
[23]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-138, PHOSPHORYLATION AT
SER-28 AND SER-32, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16973127; DOI=10.1016/j.bbrc.2006.08.160;
Littler D.R., Walker J.R., She Y.-M., Finerty P.J. Jr., Newman E.M.,
Dhe-Paganon S.;
"Structure of human protein kinase C eta (PKCeta) C2 domain and
identification of phosphorylation sites.";
Biochem. Biophys. Res. Commun. 349:1182-1189(2006).
[24]
ASSOCIATION OF VARIANT ILE-374 WITH ISCHSTR, AND CHARACTERIZATION OF
VARIANT ILE-374.
PubMed=17206144; DOI=10.1038/ng1945;
Kubo M., Hata J., Ninomiya T., Matsuda K., Yonemoto K., Nakano T.,
Matsushita T., Yamazaki K., Ohnishi Y., Saito S., Kitazono T.,
Ibayashi S., Sueishi K., Iida M., Nakamura Y., Kiyohara Y.;
"A nonsynonymous SNP in PRKCH (protein kinase C eta) increases the
risk of cerebral infarction.";
Nat. Genet. 39:212-217(2007).
[25]
VARIANTS [LARGE SCALE ANALYSIS] VAL-19; ARG-65; GLN-149; GLN-359;
ILE-374; ALA-575; ILE-594 AND SER-612.
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-independent, phospholipid- and diacylglycerol
(DAG)-dependent serine/threonine-protein kinase that is involved
in the regulation of cell differentiation in keratinocytes and
pre-B cell receptor, mediates regulation of epithelial tight
junction integrity and foam cell formation, and is required for
glioblastoma proliferation and apoptosis prevention in MCF-7
cells. In keratinocytes, binds and activates the tyrosine kinase
FYN, which in turn blocks epidermal growth factor receptor (EGFR)
signaling and leads to keratinocyte growth arrest and
differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B
complex and inhibits CDK2 kinase activity, leading to RB1
dephosphorylation and thereby G1 arrest in keratinocytes. In
association with RALA activates actin depolymerization, which is
necessary for keratinocyte differentiation. In the pre-B cell
receptor signaling, functions downstream of BLNK by up-regulating
IRF4, which in turn activates L chain gene rearrangement.
Regulates epithelial tight junctions (TJs) by phosphorylating
occludin (OCLN) on threonine residues, which is necessary for the
assembly and maintenance of TJs. In association with PLD2 and via
TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced
RGS2 down-regulation and foam cell formation. Upon PMA
stimulation, mediates glioblastoma cell proliferation by
activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-
dependent phosphorylation of ELK1. Involved in the protection of
glioblastoma cells from irradiation-induced apoptosis by
preventing caspase-9 activation. In camptothecin-treated MCF-7
cells, regulates NF-kappa-B upstream signaling by activating
IKBKB, and confers protection against DNA damage-induced
apoptosis. Promotes oncogenic functions of ATF2 in the nucleus
while blocking its apoptotic function at mitochondria.
Phosphorylates ATF2 which promotes its nuclear retention and
transcriptional activity and negatively regulates its
mitochondrial localization. {ECO:0000269|PubMed:10806212,
ECO:0000269|PubMed:11112424, ECO:0000269|PubMed:11772428,
ECO:0000269|PubMed:15489897, ECO:0000269|PubMed:17146445,
ECO:0000269|PubMed:18780722, ECO:0000269|PubMed:19114660,
ECO:0000269|PubMed:20558593, ECO:0000269|PubMed:21820409,
ECO:0000269|PubMed:22304920}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
calcium-insensitive, but activated by diacylglycerol (DAG) and
phosphatidylserine. Three specific sites; Thr-513 (activation loop
of the kinase domain), Thr-656 (turn motif) and Ser-675
(hydrophobic region), need to be phosphorylated for its full
activation.
-!- SUBUNIT: Interacts with FYN and RALA (By similarity). Interacts
with DGKQ. {ECO:0000250, ECO:0000269|PubMed:15632189}.
-!- INTERACTION:
Q16625-1:OCLN; NbExp=2; IntAct=EBI-2865850, EBI-16115673;
Q28269:OCLN (xeno); NbExp=2; IntAct=EBI-2865850, EBI-16222162;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P24723-1; Sequence=Displayed;
Name=2;
IsoId=P24723-2; Sequence=VSP_056572;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Most abundant in lung, less in heart and skin.
{ECO:0000269|PubMed:1986216}.
-!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the
C2 domain is a non-calcium binding domain.
-!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an
acute neurologic event leading to death of neural tissue of the
brain and resulting in loss of motor, sensory and/or cognitive
function. Ischemic strokes, resulting from vascular occlusion, is
considered to be a highly complex disease consisting of a group of
heterogeneous disorders with multiple genetic and environmental
risk factors. {ECO:0000269|PubMed:17206144}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
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EMBL; M55284; AAA60100.1; -; mRNA.
EMBL; AK290183; BAF82872.1; -; mRNA.
EMBL; AK296158; BAG58897.1; -; mRNA.
EMBL; AL138996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW80800.1; -; Genomic_DNA.
EMBL; CH471061; EAW80801.1; -; Genomic_DNA.
EMBL; BC037268; AAH37268.1; -; mRNA.
EMBL; S74620; AAB32724.1; -; mRNA.
CCDS; CCDS9752.1; -. [P24723-1]
PIR; A39666; A39666.
RefSeq; NP_006246.2; NM_006255.4. [P24723-1]
RefSeq; XP_016876947.1; XM_017021458.1. [P24723-2]
UniGene; Hs.333907; -.
PDB; 2FK9; X-ray; 1.75 A; A=1-138.
PDB; 3TXO; X-ray; 2.05 A; A=333-683.
PDBsum; 2FK9; -.
PDBsum; 3TXO; -.
ProteinModelPortal; P24723; -.
SMR; P24723; -.
BioGrid; 111569; 13.
DIP; DIP-44588N; -.
IntAct; P24723; 7.
MINT; MINT-3973608; -.
STRING; 9606.ENSP00000329127; -.
BindingDB; P24723; -.
ChEMBL; CHEMBL3616; -.
GuidetoPHARMACOLOGY; 1487; -.
iPTMnet; P24723; -.
PhosphoSitePlus; P24723; -.
BioMuta; PRKCH; -.
DMDM; 281185512; -.
EPD; P24723; -.
MaxQB; P24723; -.
PaxDb; P24723; -.
PeptideAtlas; P24723; -.
PRIDE; P24723; -.
DNASU; 5583; -.
Ensembl; ENST00000332981; ENSP00000329127; ENSG00000027075. [P24723-1]
Ensembl; ENST00000555082; ENSP00000450981; ENSG00000027075. [P24723-2]
GeneID; 5583; -.
KEGG; hsa:5583; -.
UCSC; uc001xfn.4; human. [P24723-1]
CTD; 5583; -.
DisGeNET; 5583; -.
EuPathDB; HostDB:ENSG00000027075.13; -.
GeneCards; PRKCH; -.
HGNC; HGNC:9403; PRKCH.
HPA; HPA026294; -.
HPA; HPA053709; -.
MalaCards; PRKCH; -.
MIM; 601367; phenotype.
MIM; 605437; gene.
neXtProt; NX_P24723; -.
OpenTargets; ENSG00000027075; -.
PharmGKB; PA33767; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P24723; -.
KO; K18051; -.
OMA; NHRQLEP; -.
OrthoDB; EOG091G0QRS; -.
PhylomeDB; P24723; -.
TreeFam; TF351133; -.
BRENDA; 2.7.11.13; 2681.
Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
Reactome; R-HSA-418597; G alpha (z) signalling events.
SABIO-RK; P24723; -.
SignaLink; P24723; -.
SIGNOR; P24723; -.
ChiTaRS; PRKCH; human.
EvolutionaryTrace; P24723; -.
GeneWiki; PRKCH; -.
GenomeRNAi; 5583; -.
PRO; PR:P24723; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000027075; -.
CleanEx; HS_PRKCH; -.
ExpressionAtlas; P24723; baseline and differential.
Genevisible; P24723; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004699; F:calcium-independent protein kinase C activity; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004697; F:protein kinase C activity; TAS:ProtInc.
GO; GO:0017160; F:Ral GTPase binding; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IMP:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0070528; P:protein kinase C signaling; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IMP:UniProtKB.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00029; C1; 2.
CDD; cd05590; STKc_nPKC_eta; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR034665; nPKC_eta.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR027431; PKC_eta.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR014376; Prot_kin_PKC_delta.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00168; C2; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000551; PKC_delta; 1.
PIRSF; PIRSF501107; Protein_kin_C_eta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00239; C2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50004; C2; 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; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Differentiation; Kinase; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
CHAIN 1 683 Protein kinase C eta type.
/FTId=PRO_0000055705.
DOMAIN 12 113 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 355 614 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 615 683 AGC-kinase C-terminal.
ZN_FING 171 222 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 245 295 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 361 369 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 479 479 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 384 384 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 28 28 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:23186163,
ECO:0000305|PubMed:16973127}.
MOD_RES 32 32 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:16973127}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000250|UniProtKB:P23298}.
MOD_RES 513 513 Phosphothreonine; by PDPK1.
{ECO:0000305}.
MOD_RES 656 656 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000250|UniProtKB:Q64617}.
VAR_SEQ 1 161 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056572.
VARIANT 19 19 A -> V (in dbSNP:rs55645551).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042312.
VARIANT 65 65 K -> R (in dbSNP:rs55737090).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042313.
VARIANT 149 149 R -> Q (in dbSNP:rs55848048).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042314.
VARIANT 359 359 R -> Q (in dbSNP:rs55818778).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042315.
VARIANT 374 374 V -> I (associated with susceptibility to
ischemic stroke; increases
autophosphorylation and kinase activity;
dbSNP:rs2230500).
{ECO:0000269|PubMed:17206144,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_034604.
VARIANT 497 497 D -> Y (in dbSNP:rs11846991).
/FTId=VAR_060736.
VARIANT 575 575 T -> A (in a aLL TEL/AML1+ sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042316.
VARIANT 594 594 T -> I (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042317.
VARIANT 612 612 P -> S (in dbSNP:rs34159231).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042318.
VARIANT 645 645 D -> V (in dbSNP:rs35561533).
/FTId=VAR_042438.
CONFLICT 96 96 Missing (in Ref. 1; AAA60100).
{ECO:0000305}.
CONFLICT 109 109 L -> R (in Ref. 1; AAA60100).
{ECO:0000305}.
CONFLICT 110 110 R -> G (in Ref. 1; AAA60100).
{ECO:0000305}.
CONFLICT 393 393 Q -> L (in Ref. 1; AAA60100).
{ECO:0000305}.
CONFLICT 472 472 D -> E (in Ref. 7; AAB32724).
{ECO:0000305}.
STRAND 8 20 {ECO:0000244|PDB:2FK9}.
HELIX 26 30 {ECO:0000244|PDB:2FK9}.
TURN 31 33 {ECO:0000244|PDB:2FK9}.
STRAND 34 37 {ECO:0000244|PDB:2FK9}.
STRAND 43 49 {ECO:0000244|PDB:2FK9}.
STRAND 52 56 {ECO:0000244|PDB:2FK9}.
STRAND 67 79 {ECO:0000244|PDB:2FK9}.
STRAND 81 88 {ECO:0000244|PDB:2FK9}.
STRAND 91 94 {ECO:0000244|PDB:2FK9}.
STRAND 96 104 {ECO:0000244|PDB:2FK9}.
HELIX 105 112 {ECO:0000244|PDB:2FK9}.
STRAND 116 123 {ECO:0000244|PDB:2FK9}.
STRAND 125 127 {ECO:0000244|PDB:2FK9}.
STRAND 129 137 {ECO:0000244|PDB:2FK9}.
STRAND 355 364 {ECO:0000244|PDB:3TXO}.
STRAND 367 374 {ECO:0000244|PDB:3TXO}.
TURN 375 377 {ECO:0000244|PDB:3TXO}.
STRAND 380 387 {ECO:0000244|PDB:3TXO}.
HELIX 388 394 {ECO:0000244|PDB:3TXO}.
HELIX 397 409 {ECO:0000244|PDB:3TXO}.
TURN 410 412 {ECO:0000244|PDB:3TXO}.
STRAND 419 424 {ECO:0000244|PDB:3TXO}.
STRAND 426 434 {ECO:0000244|PDB:3TXO}.
HELIX 441 448 {ECO:0000244|PDB:3TXO}.
HELIX 453 472 {ECO:0000244|PDB:3TXO}.
HELIX 482 484 {ECO:0000244|PDB:3TXO}.
STRAND 485 487 {ECO:0000244|PDB:3TXO}.
STRAND 493 495 {ECO:0000244|PDB:3TXO}.
HELIX 518 520 {ECO:0000244|PDB:3TXO}.
HELIX 523 530 {ECO:0000244|PDB:3TXO}.
HELIX 534 549 {ECO:0000244|PDB:3TXO}.
HELIX 559 568 {ECO:0000244|PDB:3TXO}.
HELIX 579 588 {ECO:0000244|PDB:3TXO}.
HELIX 593 595 {ECO:0000244|PDB:3TXO}.
HELIX 600 602 {ECO:0000244|PDB:3TXO}.
HELIX 606 609 {ECO:0000244|PDB:3TXO}.
HELIX 612 614 {ECO:0000244|PDB:3TXO}.
HELIX 619 623 {ECO:0000244|PDB:3TXO}.
HELIX 646 649 {ECO:0000244|PDB:3TXO}.
HELIX 663 665 {ECO:0000244|PDB:3TXO}.
HELIX 668 671 {ECO:0000244|PDB:3TXO}.
SEQUENCE 683 AA; 77828 MW; 0A29806CE31912F2 CRC64;
MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD QVRVGQTSTK
QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN CTLQFQELLR TTGASDTFEG
WVDLEPEGKV FVVITLTGSF TEATLQRDRI FKHFTRKRQR AMRRRVHQIN GHKFMATYLR
QPTYCSHCRE FIWGVFGKQG YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDSKIAEQRF
GINIPHKFSI HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV
ELAKTLAGMG LQPGNISPTS KLVSRSTLRR QGKESSKEGN GIGVNSSNRL GIDNFEFIRV
LGKGSFGKVM LARVKETGDL YAVKVLKKDV ILQDDDVECT MTEKRILSLA RNHPFLTQLF
CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR FDEARARFYA AEIISALMFL HDKGIIYRDL
KLDNVLLDHE GHCKLADFGM CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM
GVLLYEMLCG HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSFMT KNPTMRLGSL
TQGGEHAILR HPFFKEIDWA QLNHRQIEPP FRPRIKSRED VSNFDPDFIK EEPVLTPIDE
GHLPMINQDE FRNFSYVSPE LQP


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