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P24723 (KPCL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C eta type

EC=2.7.11.13
Alternative name(s):
PKC-L
nPKC-eta
Gene names
Name:PRKCH
Synonyms:PKCL, PRKCL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length683 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20

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 structure

Interacts with FYN and RALA By similarity. Interacts with DGKQ. Ref.12

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Most abundant in lung, less in heart and skin. Ref.1

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.

Involvement in 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.22

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

negative regulation of glial cell apoptotic process

Inferred from mutant phenotype Ref.10. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

positive regulation of B cell receptor signaling pathway

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of glial cell proliferation

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of keratinocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of macrophage derived foam cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase C signaling

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from mutant phenotype Ref.20. Source: UniProtKB

regulation of tight junction assembly

Inferred from mutant phenotype Ref.16. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

plasma membrane

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-independent protein kinase C activity

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction Ref.12. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 683683Protein kinase C eta type
PRO_0000055705

Regions

Domain12 – 113102C2
Domain355 – 614260Protein kinase
Domain615 – 68369AGC-kinase C-terminal
Zinc finger171 – 22252Phorbol-ester/DAG-type 1
Zinc finger245 – 29551Phorbol-ester/DAG-type 2
Nucleotide binding361 – 3699ATP By similarity

Sites

Active site4791Proton acceptor By similarity
Binding site3841ATP By similarity

Amino acid modifications

Modified residue281Phosphoserine; by autocatalysis Probable
Modified residue321Phosphoserine; by autocatalysis Probable
Modified residue3171Phosphoserine By similarity
Modified residue5131Phosphothreonine; by PDPK1 Probable
Modified residue6561Phosphothreonine Probable

Natural variations

Natural variant191A → V. Ref.23
Corresponds to variant rs55645551 [ dbSNP | Ensembl ].
VAR_042312
Natural variant651K → R. Ref.23
Corresponds to variant rs55737090 [ dbSNP | Ensembl ].
VAR_042313
Natural variant1491R → Q. Ref.23
Corresponds to variant rs55848048 [ dbSNP | Ensembl ].
VAR_042314
Natural variant3591R → Q. Ref.23
Corresponds to variant rs55818778 [ dbSNP | Ensembl ].
VAR_042315
Natural variant3741V → I Associated with susceptibility to ischemic stroke; increases autophosphorylation and kinase activity. Ref.22 Ref.23
Corresponds to variant rs2230500 [ dbSNP | Ensembl ].
VAR_034604
Natural variant4971D → Y.
Corresponds to variant rs11846991 [ dbSNP | Ensembl ].
VAR_060736
Natural variant5751T → A in a aLL TEL/AML1+ sample; somatic mutation. Ref.23
VAR_042316
Natural variant5941T → I in a colorectal adenocarcinoma sample; somatic mutation. Ref.23
VAR_042317
Natural variant6121P → S. Ref.23
Corresponds to variant rs34159231 [ dbSNP | Ensembl ].
VAR_042318
Natural variant6451D → V.
Corresponds to variant rs35561533 [ dbSNP | Ensembl ].
VAR_042438

Experimental info

Sequence conflict961Missing in AAA60100. Ref.1
Sequence conflict1091L → R in AAA60100. Ref.1
Sequence conflict1101R → G in AAA60100. Ref.1
Sequence conflict3931Q → L in AAA60100. Ref.1
Sequence conflict4721D → E in AAB32724. Ref.7

Secondary structure

............................................................................ 683
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24723 [UniParc].

Last modified December 15, 2009. Version 4.
Checksum: 0A29806CE31912F2

FASTA68377,828
        10         20         30         40         50         60 
MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD QVRVGQTSTK 

        70         80         90        100        110        120 
QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN CTLQFQELLR TTGASDTFEG 

       130        140        150        160        170        180 
WVDLEPEGKV FVVITLTGSF TEATLQRDRI FKHFTRKRQR AMRRRVHQIN GHKFMATYLR 

       190        200        210        220        230        240 
QPTYCSHCRE FIWGVFGKQG YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDSKIAEQRF 

       250        260        270        280        290        300 
GINIPHKFSI HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV 

       310        320        330        340        350        360 
ELAKTLAGMG LQPGNISPTS KLVSRSTLRR QGKESSKEGN GIGVNSSNRL GIDNFEFIRV 

       370        380        390        400        410        420 
LGKGSFGKVM LARVKETGDL YAVKVLKKDV ILQDDDVECT MTEKRILSLA RNHPFLTQLF 

       430        440        450        460        470        480 
CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR FDEARARFYA AEIISALMFL HDKGIIYRDL 

       490        500        510        520        530        540 
KLDNVLLDHE GHCKLADFGM CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM 

       550        560        570        580        590        600 
GVLLYEMLCG HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSFMT KNPTMRLGSL 

       610        620        630        640        650        660 
TQGGEHAILR HPFFKEIDWA QLNHRQIEPP FRPRIKSRED VSNFDPDFIK EEPVLTPIDE 

       670        680 
GHLPMINQDE FRNFSYVSPE LQP 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of PKC-L, a new member of the protein kinase C-related gene family specifically expressed in lung, skin, and heart."
Bacher N., Zisman Y., Berent E., Livneh E.
Mol. Cell. Biol. 11:126-133(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Lung.
[2]Erratum
Bacher N., Zisman Y., Berent E., Livneh E.
Mol. Cell. Biol. 12:1404-1404(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thalamus.
[4]"The DNA sequence and analysis of human chromosome 14."
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. expand/collapse author list , 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.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[7]"Identification of multiple, novel, protein kinase C-related gene products."
Palmer R.H., Ridden J., Parker P.J.
FEBS Lett. 356:5-8(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 438-539.
[8]"Overexpression of protein kinase C-eta attenuates caspase activation and tumor necrosis factor-alpha-induced cell death."
Akkaraju G.R., Basu A.
Biochem. Biophys. Res. Commun. 279:103-107(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Phorbol 12-myristate 13-acetate induces protein kinase ceta-specific proliferative response in astrocytic tumor cells."
Hussaini I.M., Karns L.R., Vinton G., Carpenter J.E., Redpath G.T., Sando J.J., VandenBerg S.R.
J. Biol. Chem. 275:22348-22354(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION.
[10]"Protein kinase C-eta regulates resistance to UV- and gamma-irradiation-induced apoptosis in glioblastoma cells by preventing caspase-9 activation."
Hussaini I.M., Carpenter J.E., Redpath G.T., Sando J.J., Shaffrey M.E., Vandenberg S.R.
Neuro-oncol. 4:9-21(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"PKC-eta mediates glioblastoma cell proliferation through the Akt and mTOR signaling pathways."
Aeder S.E., Martin P.M., Soh J.W., Hussaini I.M.
Oncogene 23:9062-9069(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION.
[12]"Translocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C."
van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.
J. Biol. Chem. 280:9870-9878(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DGKQ.
[13]"The protein kinase C-eta isoform induces proliferation in glioblastoma cell lines through an ERK/Elk-1 pathway."
Uht R.M., Amos S., Martin P.M., Riggan A.E., Hussaini I.M.
Oncogene 26:2885-2893(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"PKC eta directs induction of IRF-4 expression and Ig kappa gene rearrangement in pre-BCR signaling pathway."
Oda A., Ono T., Yamamoto M., Goitsuka R., Kitamura D.
Int. Immunol. 20:1417-1426(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN B-CELL SIGNALING.
[15]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"PKC eta regulates occludin phosphorylation and epithelial tight junction integrity."
Suzuki T., Elias B.C., Seth A., Shen L., Turner J.R., Giorgianni F., Desiderio D., Guntaka R., Rao R.
Proc. Natl. Acad. Sci. U.S.A. 106:61-66(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF OCLN.
[17]"Protein kinase C-eta and phospholipase D2 pathway regulates foam cell formation via regulator of G protein signaling 2."
Lee H.K., Yeo S., Kim J.S., Lee J.G., Bae Y.S., Lee C., Baek S.H.
Mol. Pharmacol. 78:478-485(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Protein kinase C? activates NF-?B in response to camptothecin-induced DNA damage."
Raveh-Amit H., Hai N., Rotem-Dai N., Shahaf G., Gopas J., Livneh E.
Biochem. Biophys. Res. Commun. 412:313-317(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Protein kinase C eta (PKC eta): its involvement in keratinocyte differentiation."
Kashiwagi M., Ohba M., Chida K., Kuroki T.
J. Biochem. 132:853-857(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[20]"PKCepsilon promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria."
Lau E., Kluger H., Varsano T., Lee K., Scheffler I., Rimm D.L., Ideker T., Ronai Z.A.
Cell 148:543-555(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites."
Littler D.R., Walker J.R., She Y.-M., Finerty P.J. Jr., Newman E.M., Dhe-Paganon S.
Biochem. Biophys. Res. Commun. 349:1182-1189(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-138, PHOSPHORYLATION AT SER-28 AND SER-32, IDENTIFICATION BY MASS SPECTROMETRY.
[22]"A nonsynonymous SNP in PRKCH (protein kinase C eta) increases the risk of cerebral infarction."
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.
Nat. Genet. 39:212-217(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT ILE-374 WITH ISCHSTR, CHARACTERIZATION OF VARIANT ILE-374.
[23]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-19; ARG-65; GLN-149; GLN-359; ILE-374; ALA-575; ILE-594 AND SER-612.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55284 mRNA. Translation: AAA60100.1.
AK290183 mRNA. Translation: BAF82872.1.
AL138996 Genomic DNA. No translation available.
AL355916 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80801.1.
BC037268 mRNA. Translation: AAH37268.1.
S74620 mRNA. Translation: AAB32724.1.
CCDSCCDS9752.1.
PIRA39666.
RefSeqNP_006246.2. NM_006255.3.
UniGeneHs.333907.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FK9X-ray1.75A1-138[»]
3TXOX-ray2.05A333-683[»]
ProteinModelPortalP24723.
SMRP24723. Positions 8-295, 320-679.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111569. 10 interactions.
DIPDIP-44588N.
IntActP24723. 4 interactions.
MINTMINT-3973608.
STRING9606.ENSP00000329127.

Chemistry

BindingDBP24723.
ChEMBLCHEMBL2093867.
GuidetoPHARMACOLOGY1487.

PTM databases

PhosphoSiteP24723.

Polymorphism databases

DMDM281185512.

Proteomic databases

MaxQBP24723.
PaxDbP24723.
PRIDEP24723.

Protocols and materials databases

DNASU5583.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332981; ENSP00000329127; ENSG00000027075.
GeneID5583.
KEGGhsa:5583.
UCSCuc001xfn.3. human.

Organism-specific databases

CTD5583.
GeneCardsGC14P061655.
HGNCHGNC:9403. PRKCH.
HPACAB001998.
HPA026294.
MIM601367. phenotype.
605437. gene.
neXtProtNX_P24723.
PharmGKBPA33767.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233022.
HOVERGENHBG108317.
InParanoidP24723.
KOK18051.
OMAHRQVEPP.
OrthoDBEOG77M8QM.
PhylomeDBP24723.
TreeFamTF351133.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
SignaLinkP24723.

Gene expression databases

ArrayExpressP24723.
BgeeP24723.
CleanExHS_PRKCH.
GenevestigatorP24723.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR027431. PKC_eta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000551. PKC_delta. 1 hit.
PIRSF501107. Protein_kin_C_eta. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKCH. human.
EvolutionaryTraceP24723.
GeneWikiPRKCH.
GenomeRNAi5583.
NextBio21652.
PROP24723.
SOURCESearch...

Entry information

Entry nameKPCL_HUMAN
AccessionPrimary (citable) accession number: P24723
Secondary accession number(s): Q16246, Q8NE03
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 15, 2009
Last modified: July 9, 2014
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM