P24723 (KPCL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	683 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
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.20
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 process	Differentiation
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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.17. 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 cascade Inferred from electronic annotation. Source: Compara regulation of tight junction assembly Inferred from mutant phenotype Ref.15. Source: UniProtKB signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium-independent protein kinase C activity Inferred from electronic annotation. Source: Compara 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 683

683

Protein kinase C eta type

PRO_0000055705

Regions

Domain

12 – 113

102

C2

Domain

355 – 614

260

Protein kinase

Domain

615 – 683

69

AGC-kinase C-terminal

Zinc finger

171 – 222

52

Phorbol-ester/DAG-type 1

Zinc finger

245 – 295

51

Phorbol-ester/DAG-type 2

Nucleotide binding

361 – 369

9

ATP By similarity

Sites

Active site

479

1

Proton acceptor By similarity

Binding site

384

1

ATP By similarity

Amino acid modifications

Modified residue

28

1

Phosphoserine; by autocatalysis Probable

Modified residue

32

1

Phosphoserine; by autocatalysis Probable

Modified residue

513

1

Phosphothreonine; by PDPK1 Probable

Modified residue

656

1

Phosphothreonine Probable

Natural variations

Natural variant

19

1

A → V. Ref.21
Corresponds to variant rs55645551 [ dbSNP | Ensembl ].

VAR_042312

Natural variant

65

1

K → R. Ref.21
Corresponds to variant rs55737090 [ dbSNP | Ensembl ].

VAR_042313

Natural variant

149

1

R → Q. Ref.21
Corresponds to variant rs55848048 [ dbSNP | Ensembl ].

VAR_042314

Natural variant

359

1

R → Q. Ref.21
Corresponds to variant rs55818778 [ dbSNP | Ensembl ].

VAR_042315

Natural variant

374

1

V → I Associated with susceptibility to ischemic stroke; increases autophosphorylation and kinase activity. Ref.20 Ref.21
Corresponds to variant rs2230500 [ dbSNP | Ensembl ].

VAR_034604

Natural variant

497

1

D → Y.
Corresponds to variant rs11846991 [ dbSNP | Ensembl ].

VAR_060736

Natural variant

575

1

T → A in a aLL TEL/AML1+ sample; somatic mutation. Ref.21

VAR_042316

Natural variant

594

1

T → I in a colorectal adenocarcinoma sample; somatic mutation. Ref.21

VAR_042317

Natural variant

612

1

P → S. Ref.21
Corresponds to variant rs34159231 [ dbSNP | Ensembl ].

VAR_042318

Natural variant

645

1

D → V.
Corresponds to variant rs35561533 [ dbSNP | Ensembl ].

VAR_042438

Experimental info

Sequence conflict

96

1

Missing in AAA60100. Ref.1

Sequence conflict

109

1

L → R in AAA60100. Ref.1

Sequence conflict

110

1

R → G in AAA60100. Ref.1

Sequence conflict

393

1

Q → L in AAA60100. Ref.1

Sequence conflict

472

1

D → E in AAB32724. Ref.7

Secondary structure

1

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683

Helix Strand Turn

Details...

Beta strand

8 – 20

13

Helix

26 – 30

5

Turn

31 – 33

3

Beta strand

34 – 37

4

Beta strand

43 – 49

7

Beta strand

52 – 56

5

Beta strand

67 – 79

13

Beta strand

81 – 88

8

Beta strand

91 – 94

4

Beta strand

96 – 104

9

Helix

105 – 112

8

Beta strand

116 – 123

8

Beta strand

125 – 127

3

Beta strand

129 – 137

9

Beta strand

355 – 364

10

Beta strand

367 – 374

8

Turn

375 – 377

3

Beta strand

380 – 387

8

Helix

388 – 394

7

Helix

397 – 409

13

Turn

410 – 412

3

Beta strand

419 – 424

6

Beta strand

426 – 434

9

Helix

441 – 448

8

Helix

453 – 472

20

Helix

482 – 484

3

Beta strand

485 – 487

3

Beta strand

493 – 495

3

Helix

518 – 520

3

Helix

523 – 530

8

Helix

534 – 549

16

Helix

559 – 568

10

Helix

579 – 588

10

Helix

593 – 595

3

Helix

600 – 602

3

Helix

606 – 609

4

Helix

612 – 614

3

Helix

619 – 623

5

Helix

646 – 649

4

Helix

663 – 665

3

Helix

668 – 671

4

Sequences

	Sequence		Length	Mass (Da)
	P24723 [UniParc]. Last modified December 15, 2009. Version 4. Checksum: 0A29806CE31912F2	FASTA	683	77,828
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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, MASS SPECTROMETRY.
[20]	"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.
[21]	"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. , 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.

IPI

IPI00184572.

PIR

A39666.

RefSeq

NP_006246.2. NM_006255.3.

UniGene

Hs.333907.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FK9	X-ray	1.75	A	1-138	[»]
3TXO	X-ray	2.05	A	333-683	[»]

ProteinModelPortal

P24723.

SMR

P24723. Positions 8-298, 320-679.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44588N.

IntAct

P24723. 3 interactions.

MINT

MINT-3973608.

STRING

9606.ENSP00000329127.

PTM databases

PhosphoSite

P24723.

Polymorphism databases

DMDM

281185512.

Proteomic databases

PaxDb

P24723.

PRIDE

P24723.

Protocols and materials databases

DNASU

5583.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000332981; ENSP00000329127; ENSG00000027075.

GeneID

5583.

KEGG

hsa:5583.

UCSC

uc001xfn.3. human.

Organism-specific databases

CTD

5583.

GeneCards

GC14P061655.

HGNC

HGNC:9403. PRKCH.

HPA

CAB001998.
HPA026294.

MIM

601367. phenotype.
605437. gene.

neXtProt

NX_P24723.

PharmGKB

PA33767.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233022.

HOVERGEN

HBG108317.

InParanoid

P24723.

KO

K06068.

OMA

FSVHNYK.

OrthoDB

EOG4P2Q1P.

PhylomeDB

P24723.

Enzyme and pathway databases

BRENDA

2.7.11.13. 2681.

Pathway_Interaction_DB

endothelinpathway. Endothelins.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

SignaLink

P24723.

Gene expression databases

ArrayExpress

P24723.

Bgee

P24723.

CleanEx

HS_PRKCH.

Genevestigator

P24723.

GermOnline

ENSG00000027075. Homo sapiens.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
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_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000551. PKC_delta. 1 hit.
PIRSF501107. Protein_kin_C_eta. 1 hit.

PRINTS

PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. 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]

ProtoNet

Search...

Other

BindingDB

P24723.

ChEMBL

CHEMBL3616.

ChiTaRS

PRKCH. human.

EvolutionaryTrace

P24723.

GenomeRNAi

5583.

NextBio

21652.

SOURCE

Search...

Entry information

Entry name

KPCL_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 140 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.