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P24723

- KPCL_HUMAN

UniProt

P24723 - KPCL_HUMAN

Protein

Protein kinase C eta type

Gene

PRKCH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 4 (15 Dec 2009)
      Previous versions | rss
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    Functioni

    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.10 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei384 – 3841ATPPROSITE-ProRule annotation
    Active sitei479 – 4791Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri171 – 22252Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri245 – 29551Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi361 – 3699ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium-independent protein kinase C activity Source: Ensembl
    3. enzyme binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. protein kinase C activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. negative regulation of glial cell apoptotic process Source: UniProtKB
    3. platelet activation Source: Reactome
    4. positive regulation of B cell receptor signaling pathway Source: UniProtKB
    5. positive regulation of glial cell proliferation Source: UniProtKB
    6. positive regulation of keratinocyte differentiation Source: UniProtKB
    7. positive regulation of macrophage derived foam cell differentiation Source: UniProtKB
    8. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    9. protein kinase C signaling Source: Ensembl
    10. protein phosphorylation Source: UniProtKB
    11. regulation of tight junction assembly Source: UniProtKB
    12. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Differentiation

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_19333. G alpha (z) signalling events.
    REACT_2202. Effects of PIP2 hydrolysis.
    SignaLinkiP24723.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C eta type (EC:2.7.11.13)
    Alternative name(s):
    PKC-L
    nPKC-eta
    Gene namesi
    Name:PRKCH
    Synonyms:PKCL, PRKCL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9403. PRKCH.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi601367. phenotype.
    PharmGKBiPA33767.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 683683Protein kinase C eta typePRO_0000055705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281Phosphoserine; by autocatalysis1 Publication
    Modified residuei32 – 321Phosphoserine; by autocatalysis1 Publication
    Modified residuei317 – 3171PhosphoserineBy similarity
    Modified residuei513 – 5131Phosphothreonine; by PDPK1Curated
    Modified residuei656 – 6561PhosphothreonineCurated

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP24723.
    PaxDbiP24723.
    PRIDEiP24723.

    PTM databases

    PhosphoSiteiP24723.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP24723.
    BgeeiP24723.
    CleanExiHS_PRKCH.
    GenevestigatoriP24723.

    Organism-specific databases

    HPAiCAB001998.
    HPA026294.

    Interactioni

    Subunit structurei

    Interacts with FYN and RALA By similarity. Interacts with DGKQ.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi111569. 10 interactions.
    DIPiDIP-44588N.
    IntActiP24723. 4 interactions.
    MINTiMINT-3973608.
    STRINGi9606.ENSP00000329127.

    Structurei

    Secondary structure

    1
    683
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 2013
    Helixi26 – 305
    Turni31 – 333
    Beta strandi34 – 374
    Beta strandi43 – 497
    Beta strandi52 – 565
    Beta strandi67 – 7913
    Beta strandi81 – 888
    Beta strandi91 – 944
    Beta strandi96 – 1049
    Helixi105 – 1128
    Beta strandi116 – 1238
    Beta strandi125 – 1273
    Beta strandi129 – 1379
    Beta strandi355 – 36410
    Beta strandi367 – 3748
    Turni375 – 3773
    Beta strandi380 – 3878
    Helixi388 – 3947
    Helixi397 – 40913
    Turni410 – 4123
    Beta strandi419 – 4246
    Beta strandi426 – 4349
    Helixi441 – 4488
    Helixi453 – 47220
    Helixi482 – 4843
    Beta strandi485 – 4873
    Beta strandi493 – 4953
    Helixi518 – 5203
    Helixi523 – 5308
    Helixi534 – 54916
    Helixi559 – 56810
    Helixi579 – 58810
    Helixi593 – 5953
    Helixi600 – 6023
    Helixi606 – 6094
    Helixi612 – 6143
    Helixi619 – 6235
    Helixi646 – 6494
    Helixi663 – 6653
    Helixi668 – 6714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FK9X-ray1.75A1-138[»]
    3TXOX-ray2.05A333-683[»]
    ProteinModelPortaliP24723.
    SMRiP24723. Positions 8-295, 320-679.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24723.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 113102C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini355 – 614260Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 68369AGC-kinase C-terminalAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri171 – 22252Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri245 – 29551Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233022.
    HOVERGENiHBG108317.
    InParanoidiP24723.
    KOiK18051.
    OMAiHRQVEPP.
    OrthoDBiEOG77M8QM.
    PhylomeDBiP24723.
    TreeFamiTF351133.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000961. 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]
    PfamiPF00130. C1_1. 2 hits.
    PF00168. C2. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000551. PKC_delta. 1 hit.
    PIRSF501107. Protein_kin_C_eta. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00239. C2. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P24723-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD    50
    QVRVGQTSTK QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN 100
    CTLQFQELLR TTGASDTFEG WVDLEPEGKV FVVITLTGSF TEATLQRDRI 150
    FKHFTRKRQR AMRRRVHQIN GHKFMATYLR QPTYCSHCRE FIWGVFGKQG 200
    YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDSKIAEQRF GINIPHKFSI 250
    HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV 300
    ELAKTLAGMG LQPGNISPTS KLVSRSTLRR QGKESSKEGN GIGVNSSNRL 350
    GIDNFEFIRV LGKGSFGKVM LARVKETGDL YAVKVLKKDV ILQDDDVECT 400
    MTEKRILSLA RNHPFLTQLF CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR 450
    FDEARARFYA AEIISALMFL HDKGIIYRDL KLDNVLLDHE GHCKLADFGM 500
    CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM GVLLYEMLCG 550
    HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSFMT KNPTMRLGSL 600
    TQGGEHAILR HPFFKEIDWA QLNHRQIEPP FRPRIKSRED VSNFDPDFIK 650
    EEPVLTPIDE GHLPMINQDE FRNFSYVSPE LQP 683
    Length:683
    Mass (Da):77,828
    Last modified:December 15, 2009 - v4
    Checksum:i0A29806CE31912F2
    GO
    Isoform 2 (identifier: P24723-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-161: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:522
    Mass (Da):59,521
    Checksum:iD6852F6089A763E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961Missing in AAA60100. (PubMed:1986216)Curated
    Sequence conflicti109 – 1091L → R in AAA60100. (PubMed:1986216)Curated
    Sequence conflicti110 – 1101R → G in AAA60100. (PubMed:1986216)Curated
    Sequence conflicti393 – 3931Q → L in AAA60100. (PubMed:1986216)Curated
    Sequence conflicti472 – 4721D → E in AAB32724. (PubMed:7988719)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191A → V.1 Publication
    Corresponds to variant rs55645551 [ dbSNP | Ensembl ].
    VAR_042312
    Natural varianti65 – 651K → R.1 Publication
    Corresponds to variant rs55737090 [ dbSNP | Ensembl ].
    VAR_042313
    Natural varianti149 – 1491R → Q.1 Publication
    Corresponds to variant rs55848048 [ dbSNP | Ensembl ].
    VAR_042314
    Natural varianti359 – 3591R → Q.1 Publication
    Corresponds to variant rs55818778 [ dbSNP | Ensembl ].
    VAR_042315
    Natural varianti374 – 3741V → I Associated with susceptibility to ischemic stroke; increases autophosphorylation and kinase activity. 1 Publication
    Corresponds to variant rs2230500 [ dbSNP | Ensembl ].
    VAR_034604
    Natural varianti497 – 4971D → Y.
    Corresponds to variant rs11846991 [ dbSNP | Ensembl ].
    VAR_060736
    Natural varianti575 – 5751T → A in a aLL TEL/AML1+ sample; somatic mutation. 1 Publication
    VAR_042316
    Natural varianti594 – 5941T → I in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042317
    Natural varianti612 – 6121P → S.1 Publication
    Corresponds to variant rs34159231 [ dbSNP | Ensembl ].
    VAR_042318
    Natural varianti645 – 6451D → V.
    Corresponds to variant rs35561533 [ dbSNP | Ensembl ].
    VAR_042438

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 161161Missing in isoform 2. 1 PublicationVSP_056572Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55284 mRNA. Translation: AAA60100.1.
    AK290183 mRNA. Translation: BAF82872.1.
    AK296158 mRNA. Translation: BAG58897.1.
    AL138996 Genomic DNA. No translation available.
    AL355916 Genomic DNA. No translation available.
    AL359220 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW80800.1.
    CH471061 Genomic DNA. Translation: EAW80801.1.
    BC037268 mRNA. Translation: AAH37268.1.
    S74620 mRNA. Translation: AAB32724.1.
    CCDSiCCDS9752.1.
    PIRiA39666.
    RefSeqiNP_006246.2. NM_006255.4.
    UniGeneiHs.333907.

    Genome annotation databases

    EnsembliENST00000332981; ENSP00000329127; ENSG00000027075.
    ENST00000555082; ENSP00000450981; ENSG00000027075.
    GeneIDi5583.
    KEGGihsa:5583.
    UCSCiuc001xfn.3. human.

    Polymorphism databases

    DMDMi281185512.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55284 mRNA. Translation: AAA60100.1 .
    AK290183 mRNA. Translation: BAF82872.1 .
    AK296158 mRNA. Translation: BAG58897.1 .
    AL138996 Genomic DNA. No translation available.
    AL355916 Genomic DNA. No translation available.
    AL359220 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW80800.1 .
    CH471061 Genomic DNA. Translation: EAW80801.1 .
    BC037268 mRNA. Translation: AAH37268.1 .
    S74620 mRNA. Translation: AAB32724.1 .
    CCDSi CCDS9752.1.
    PIRi A39666.
    RefSeqi NP_006246.2. NM_006255.4.
    UniGenei Hs.333907.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FK9 X-ray 1.75 A 1-138 [» ]
    3TXO X-ray 2.05 A 333-683 [» ]
    ProteinModelPortali P24723.
    SMRi P24723. Positions 8-295, 320-679.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111569. 10 interactions.
    DIPi DIP-44588N.
    IntActi P24723. 4 interactions.
    MINTi MINT-3973608.
    STRINGi 9606.ENSP00000329127.

    Chemistry

    BindingDBi P24723.
    ChEMBLi CHEMBL2093867.
    GuidetoPHARMACOLOGYi 1487.

    PTM databases

    PhosphoSitei P24723.

    Polymorphism databases

    DMDMi 281185512.

    Proteomic databases

    MaxQBi P24723.
    PaxDbi P24723.
    PRIDEi P24723.

    Protocols and materials databases

    DNASUi 5583.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332981 ; ENSP00000329127 ; ENSG00000027075 .
    ENST00000555082 ; ENSP00000450981 ; ENSG00000027075 .
    GeneIDi 5583.
    KEGGi hsa:5583.
    UCSCi uc001xfn.3. human.

    Organism-specific databases

    CTDi 5583.
    GeneCardsi GC14P061655.
    HGNCi HGNC:9403. PRKCH.
    HPAi CAB001998.
    HPA026294.
    MIMi 601367. phenotype.
    605437. gene.
    neXtProti NX_P24723.
    PharmGKBi PA33767.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233022.
    HOVERGENi HBG108317.
    InParanoidi P24723.
    KOi K18051.
    OMAi HRQVEPP.
    OrthoDBi EOG77M8QM.
    PhylomeDBi P24723.
    TreeFami TF351133.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 2681.
    Reactomei REACT_19333. G alpha (z) signalling events.
    REACT_2202. Effects of PIP2 hydrolysis.
    SignaLinki P24723.

    Miscellaneous databases

    ChiTaRSi PRKCH. human.
    EvolutionaryTracei P24723.
    GeneWikii PRKCH.
    GenomeRNAii 5583.
    NextBioi 21652.
    PROi P24723.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24723.
    Bgeei P24723.
    CleanExi HS_PRKCH.
    Genevestigatori P24723.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000961. 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 ]
    Pfami PF00130. C1_1. 2 hits.
    PF00168. C2. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000551. PKC_delta. 1 hit.
    PIRSF501107. Protein_kin_C_eta. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00239. C2. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1), 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] (ISOFORMS 1 AND 2).
      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. 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] (ISOFORM 1).
      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 (ISOFORM 1).
    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. 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.
      , 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.

    Entry informationi

    Entry nameiKPCL_HUMAN
    AccessioniPrimary (citable) accession number: P24723
    Secondary accession number(s): B4DJN5, Q16246, Q8NE03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: December 15, 2009
    Last modified: October 1, 2014
    This is version 154 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3