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P24723

- KPCL_HUMAN

UniProt

P24723 - KPCL_HUMAN

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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

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
Complete GO annotation...

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. cell-cell junction Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

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

BgeeiP24723.
CleanExiHS_PRKCH.
ExpressionAtlasiP24723. baseline and differential.
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.
GeneTreeiENSGT00760000118891.
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.
IPR002219. PE/DAG-bd.
IPR027431. PKC_eta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

        10         20         30         40         50
MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD
60 70 80 90 100
QVRVGQTSTK QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN
110 120 130 140 150
CTLQFQELLR TTGASDTFEG WVDLEPEGKV FVVITLTGSF TEATLQRDRI
160 170 180 190 200
FKHFTRKRQR AMRRRVHQIN GHKFMATYLR QPTYCSHCRE FIWGVFGKQG
210 220 230 240 250
YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDSKIAEQRF GINIPHKFSI
260 270 280 290 300
HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV
310 320 330 340 350
ELAKTLAGMG LQPGNISPTS KLVSRSTLRR QGKESSKEGN GIGVNSSNRL
360 370 380 390 400
GIDNFEFIRV LGKGSFGKVM LARVKETGDL YAVKVLKKDV ILQDDDVECT
410 420 430 440 450
MTEKRILSLA RNHPFLTQLF CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR
460 470 480 490 500
FDEARARFYA AEIISALMFL HDKGIIYRDL KLDNVLLDHE GHCKLADFGM
510 520 530 540 550
CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM GVLLYEMLCG
560 570 580 590 600
HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSFMT KNPTMRLGSL
610 620 630 640 650
TQGGEHAILR HPFFKEIDWA QLNHRQIEPP FRPRIKSRED VSNFDPDFIK
660 670 680
EEPVLTPIDE GHLPMINQDE FRNFSYVSPE LQP
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. [P24723-1]
PIRiA39666.
RefSeqiNP_006246.2. NM_006255.4.
UniGeneiHs.333907.

Genome annotation databases

EnsembliENST00000332981; ENSP00000329127; ENSG00000027075. [P24723-1]
ENST00000555082; ENSP00000450981; ENSG00000027075. [P24723-2]
GeneIDi5583.
KEGGihsa:5583.
UCSCiuc001xfn.3. human. [P24723-1]

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. [P24723-1 ]
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 CHEMBL3616.
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 . [P24723-1 ]
ENST00000555082 ; ENSP00000450981 ; ENSG00000027075 . [P24723-2 ]
GeneIDi 5583.
KEGGi hsa:5583.
UCSCi uc001xfn.3. human. [P24723-1 ]

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.
GeneTreei ENSGT00760000118891.
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

Bgeei P24723.
CleanExi HS_PRKCH.
ExpressionAtlasi P24723. baseline and differential.
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.
IPR002219. PE/DAG-bd.
IPR027431. PKC_eta.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 155 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