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Protein

Protein kinase C epsilon type

Gene

PRKCE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. In HeLa cells, contributes to hepatocyte growth factor (HGF)-induced cell migration, and in human corneal epithelial cells, plays a critical role in wound healing after activation by HGF. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). In prostate cancer cells, interacts with and phosphorylates STAT3, which increases DNA-binding and transcriptional activity of STAT3 and seems to be essential for prostate cancer cell invasion. Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1.7 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-566 (activation loop of the kinase domain), Thr-710 (turn motif) and Ser-729 (hydrophobic region), need to be phosphorylated for its full activation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei437ATPPROSITE-ProRule annotation1
Active sitei532Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri169 – 220Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri242 – 292Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
Nucleotide bindingi414 – 422ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • actin monomer binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • calcium-independent protein kinase C activity Source: Ensembl
  • enzyme activator activity Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • ethanol binding Source: Ensembl
  • metal ion binding Source: UniProtKB-KW
  • protein kinase C activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: UniProtKB
  • receptor activator activity Source: Ensembl
  • signal transducer activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell adhesion, Cell cycle, Cell division, Immunity

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS10253-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-1250196. SHC1 events in ERBB2 signaling.
R-HSA-1489509. DAG and IP3 signaling.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-418597. G alpha (z) signalling events.
SABIO-RKQ02156.
SignaLinkiQ02156.
SIGNORiQ02156.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C epsilon type (EC:2.7.11.13)
Alternative name(s):
nPKC-epsilon
Gene namesi
Name:PRKCE
Synonyms:PKCE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:9401. PRKCE.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeleton 1 Publication
  • Cell membrane 1 Publication
  • Cytoplasmperinuclear region By similarity
  • Nucleus By similarity

  • Note: Translocated to plasma membrane in epithelial cells stimulated by HGF. Associated with the Golgi at the perinuclear site in pre-passage fibroblasts (By similarity). In passaging cells, translocated to the cell periphery (By similarity). Translocated to the nucleus in PMA-treated cells (By similarity).By similarity

GO - Cellular componenti

  • cell periphery Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: BHF-UCL
  • Golgi apparatus Source: Ensembl
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi437K → W: Abolishes activity and S-729 phosphorylation. 1 Publication1
Mutagenesisi566T → A: Abolishes phosphorylation by PDK1, and S-729 phosphorylation. 1 Publication1
Mutagenesisi566T → E: No effect on S-729 phosphorylation. 1 Publication1
Mutagenesisi710T → E: No effect on activity; no effect on S-729 phosphorylation. 1 Publication1
Mutagenesisi729S → A: Enhances T-566 dephosphorylation. 1 Publication1

Organism-specific databases

DisGeNETi5581.
OpenTargetsiENSG00000171132.
PharmGKBiPA33765.

Chemistry databases

ChEMBLiCHEMBL3582.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1486.

Polymorphism and mutation databases

BioMutaiPRKCE.
DMDMi400135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000556971 – 737Protein kinase C epsilon typeAdd BLAST737

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei62PhosphoserineBy similarity1
Modified residuei228PhosphothreonineCombined sources1
Modified residuei234PhosphoserineBy similarity1
Modified residuei309PhosphothreonineCombined sources1
Modified residuei316PhosphoserineCombined sources1
Modified residuei329PhosphoserineCombined sources1
Modified residuei337PhosphoserineBy similarity1
Modified residuei346Phosphoserine; by GSK3-beta1 Publication1
Modified residuei349PhosphothreonineBy similarity1
Modified residuei350Phosphoserine; by MAPK11 and MAPK14Curated1
Modified residuei368Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei388PhosphoserineCombined sources1
Modified residuei566Phosphothreonine; by PDPK11 Publication1
Modified residuei703Phosphothreonine; by autocatalysisSequence analysis1
Modified residuei710PhosphothreonineCombined sources1
Modified residuei729Phosphoserine; by autocatalysis1 Publication1

Post-translational modificationi

Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729. Phosphorylation in the hinge domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-368 by autophosphorylation is required for interaction with YWHAB.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ02156.
MaxQBiQ02156.
PaxDbiQ02156.
PeptideAtlasiQ02156.
PRIDEiQ02156.

PTM databases

iPTMnetiQ02156.
PhosphoSitePlusiQ02156.

Miscellaneous databases

PMAP-CutDBQ02156.

Expressioni

Gene expression databases

BgeeiENSG00000171132.
CleanExiHS_PRKCE.
ExpressionAtlasiQ02156. baseline and differential.
GenevisibleiQ02156. HS.

Organism-specific databases

HPAiCAB001948.
HPA044496.

Interactioni

Subunit structurei

Forms a ternary complex with TRIM63 and GN2BL1. Can form a complex with PDLIM5 and N-type calcium channel. Interacts with COPB1 and YWHAB (By similarity). Interacts with DGKQ and STAT3.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-706254,EBI-352572
IL32C6GKH12EBI-706254,EBI-9547476
RPS6KA2Q153492EBI-706254,EBI-1384149
YWHAZP631045EBI-706254,EBI-347088

GO - Molecular functioni

  • actin monomer binding Source: UniProtKB
  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111567. 52 interactors.
DIPiDIP-34186N.
IntActiQ02156. 13 interactors.
MINTiMINT-88515.
STRINGi9606.ENSP00000306124.

Chemistry databases

BindingDBiQ02156.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WH0X-ray2.25Q/R342-372[»]
5LIHX-ray3.25F/G149-164[»]
ProteinModelPortaliQ02156.
SMRiQ02156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02156.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 99C2PROSITE-ProRule annotationAdd BLAST99
Domaini408 – 668Protein kinasePROSITE-ProRule annotationAdd BLAST261
Domaini669 – 737AGC-kinase C-terminalAdd BLAST69

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi223 – 228Interaction with actinBy similarity6

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)DescriptionActionsGraphical viewLength
Zinc fingeri169 – 220Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri242 – 292Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiQ02156.
KOiK18050.
OMAiDEDVDCT.
OrthoDBiEOG091G0QRS.
PhylomeDBiQ02156.
TreeFamiTF351133.

Family and domain databases

CDDicd00029. C1. 2 hits.
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.
IPR027274. PKC_epsilon.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.
PIRSF501106. Protein_kin_C_epsilon. 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]

Sequencei

Sequence statusi: Complete.

Q02156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR
60 70 80 90 100
IGQTATKQKT NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI
110 120 130 140 150
QFEELLQNGS RHFEDWIDLE PEGRVYVIID LSGSSGEAPK DNEERVFRER
160 170 180 190 200
MRPRKRQGAV RRRVHQVNGH KFMATYLRQP TYCSHCRDFI WGVIGKQGYQ
210 220 230 240 250
CQVCTCVVHK RCHELIITKC AGLKKQETPD QVGSQRFSVN MPHKFGIHNY
260 270 280 290 300
KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
310 320 330 340 350
KVLADLGVTP DKITNSGQRR KKLIAGAESP QPASGSSPSE EDRSKSAPTS
360 370 380 390 400
PCDQEIKELE NNIRKALSFD NRGEEHRAAS SPDGQLMSPG ENGEVRQGQA
410 420 430 440 450
KRLGLDEFNF IKVLGKGSFG KVMLAELKGK DEVYAVKVLK KDVILQDDDV
460 470 480 490 500
DCTMTEKRIL ALARKHPYLT QLYCCFQTKD RLFFVMEYVN GGDLMFQIQR
510 520 530 540 550
SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL DAEGHCKLAD
560 570 580 590 600
FGMCKEGILN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM
610 620 630 640 650
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL
660 670 680 690 700
GCVASQNGED AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ
710 720 730
DFTREEPVLT LVDEAIVKQI NQEEFKGFSY FGEDLMP
Length:737
Mass (Da):83,674
Last modified:July 1, 1993 - v1
Checksum:i85032D0A091A1F7F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035466143E → K in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs772834505dbSNPEnsembl.1
Natural variantiVAR_042307333A → V.1 PublicationCorresponds to variant rs55989965dbSNPEnsembl.1
Natural variantiVAR_042308389P → R.1 PublicationCorresponds to variant rs55767130dbSNPEnsembl.1
Natural variantiVAR_042309563T → M.1 PublicationCorresponds to variant rs34077350dbSNPEnsembl.1
Natural variantiVAR_050559654A → T.Corresponds to variant rs35777875dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65293 mRNA. Translation: CAA46388.1.
EU332867 Genomic DNA. Translation: ABY87556.1.
U51244 Genomic DNA. Translation: AAD08855.1.
AC017078 Genomic DNA. Translation: AAY14773.1.
AC017006 Genomic DNA. Translation: AAX93253.1.
CH471053 Genomic DNA. Translation: EAX00258.1.
BC109033 mRNA. Translation: AAI09034.1.
BC109034 mRNA. Translation: AAI09035.1.
CCDSiCCDS1824.1.
PIRiS28942.
RefSeqiNP_005391.1. NM_005400.2.
XP_005264485.1. XM_005264428.1.
UniGeneiHs.580351.
Hs.677120.

Genome annotation databases

EnsembliENST00000306156; ENSP00000306124; ENSG00000171132.
GeneIDi5581.
KEGGihsa:5581.
UCSCiuc002rut.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65293 mRNA. Translation: CAA46388.1.
EU332867 Genomic DNA. Translation: ABY87556.1.
U51244 Genomic DNA. Translation: AAD08855.1.
AC017078 Genomic DNA. Translation: AAY14773.1.
AC017006 Genomic DNA. Translation: AAX93253.1.
CH471053 Genomic DNA. Translation: EAX00258.1.
BC109033 mRNA. Translation: AAI09034.1.
BC109034 mRNA. Translation: AAI09035.1.
CCDSiCCDS1824.1.
PIRiS28942.
RefSeqiNP_005391.1. NM_005400.2.
XP_005264485.1. XM_005264428.1.
UniGeneiHs.580351.
Hs.677120.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WH0X-ray2.25Q/R342-372[»]
5LIHX-ray3.25F/G149-164[»]
ProteinModelPortaliQ02156.
SMRiQ02156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111567. 52 interactors.
DIPiDIP-34186N.
IntActiQ02156. 13 interactors.
MINTiMINT-88515.
STRINGi9606.ENSP00000306124.

Chemistry databases

BindingDBiQ02156.
ChEMBLiCHEMBL3582.
DrugBankiDB00675. Tamoxifen.
GuidetoPHARMACOLOGYi1486.

PTM databases

iPTMnetiQ02156.
PhosphoSitePlusiQ02156.

Polymorphism and mutation databases

BioMutaiPRKCE.
DMDMi400135.

Proteomic databases

EPDiQ02156.
MaxQBiQ02156.
PaxDbiQ02156.
PeptideAtlasiQ02156.
PRIDEiQ02156.

Protocols and materials databases

DNASUi5581.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306156; ENSP00000306124; ENSG00000171132.
GeneIDi5581.
KEGGihsa:5581.
UCSCiuc002rut.4. human.

Organism-specific databases

CTDi5581.
DisGeNETi5581.
GeneCardsiPRKCE.
HGNCiHGNC:9401. PRKCE.
HPAiCAB001948.
HPA044496.
MIMi176975. gene.
neXtProtiNX_Q02156.
OpenTargetsiENSG00000171132.
PharmGKBiPA33765.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiQ02156.
KOiK18050.
OMAiDEDVDCT.
OrthoDBiEOG091G0QRS.
PhylomeDBiQ02156.
TreeFamiTF351133.

Enzyme and pathway databases

BioCyciZFISH:HS10253-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-114508. Effects of PIP2 hydrolysis.
R-HSA-1250196. SHC1 events in ERBB2 signaling.
R-HSA-1489509. DAG and IP3 signaling.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-418597. G alpha (z) signalling events.
SABIO-RKQ02156.
SignaLinkiQ02156.
SIGNORiQ02156.

Miscellaneous databases

ChiTaRSiPRKCE. human.
EvolutionaryTraceiQ02156.
GeneWikiiPRKCE.
GenomeRNAii5581.
PMAP-CutDBQ02156.
PROiQ02156.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171132.
CleanExiHS_PRKCE.
ExpressionAtlasiQ02156. baseline and differential.
GenevisibleiQ02156. HS.

Family and domain databases

CDDicd00029. C1. 2 hits.
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.
IPR027274. PKC_epsilon.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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.
PIRSF501106. Protein_kin_C_epsilon. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiKPCE_HUMAN
AccessioniPrimary (citable) accession number: Q02156
Secondary accession number(s): B0LPH7
, Q32MQ3, Q53SL4, Q53SM5, Q9UE81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 175 of the entry and version 1 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 2
    Human chromosome 2: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.