Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P16054 (KPCE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C epsilon type

EC=2.7.11.13
Alternative name(s):
nPKC-epsilon
Gene names
Name:Prkce
Synonyms:Pkce, Pkcea
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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). 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. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13

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-566 (activation loop of the kinase domain), Thr-710 (turn motif) and Ser-729 (hydrophobic region), need to be phosphorylated for its full activation.

Subunit structure

Forms a ternary complex with TRIM63 and GN2BL1. Can form a complex with PDLIM5 and N-type calcium channel. Interacts with COPB1, DGKQ and STAT3 By similarity. Interacts with YWHAB. Ref.4 Ref.13

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity. Cytoplasmperinuclear region. Nucleus. Note: Translocated to plasma membrane in epithelial cells stimulated by HGF By similarity. Associated with the Golgi at the perinuclear site in pre-passage fibroblasts. In passaging cells, translocated to the cell periphery. Translocated to the nucleus in PMA-treated cells. Ref.11

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.

Post-translational modification

Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729 By similarity. 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.

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 processCell adhesion
Cell cycle
Cell division
Immunity
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   DomainRepeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processTRAM-dependent toll-like receptor 4 signaling pathway

Inferred from mutant phenotype Ref.10. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to ethanol

Inferred from genetic interaction PubMed 17875639. Source: MGI

cellular response to hypoxia

Inferred from direct assay PubMed 18070622. Source: MGI

chemosensory behavior

Traceable author statement PubMed 11606660. Source: MGI

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipopolysaccharide-mediated signaling pathway

Inferred from mutant phenotype Ref.10. Source: UniProtKB

locomotory exploration behavior

Inferred from genetic interaction PubMed 17908177. Source: MGI

macrophage activation involved in immune response

Inferred from mutant phenotype PubMed 11696589. Source: MGI

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 11696589. Source: MGI

positive regulation of MAPK cascade

Inferred from direct assay PubMed 11884367. Source: MGI

positive regulation of actin filament polymerization

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of cell-substrate adhesion

Inferred from mutant phenotype Ref.7. Source: MGI

positive regulation of cellular glucuronidation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of fibroblast migration

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of insulin secretion

Inferred from mutant phenotype PubMed 12837755. Source: MGI

positive regulation of lipid catabolic process

Inferred from mutant phenotype PubMed 19401415. Source: MGI

positive regulation of mucus secretion

Inferred from mutant phenotype PubMed 17728398. Source: MGI

positive regulation of receptor activity

Inferred from direct assay PubMed 17875639. Source: GOC

positive regulation of synaptic transmission, GABAergic

Inferred from mutant phenotype PubMed 17875639. Source: MGI

positive regulation of wound healing

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 12551921. Source: MGI

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 19401415. Source: MGI

regulation of lipid metabolic process

Inferred from mutant phenotype PubMed 19401415. Source: MGI

regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 11940581. Source: MGI

release of sequestered calcium ion into cytosol

Inferred from mutant phenotype PubMed 15905535. Source: MGI

response to morphine

Inferred from mutant phenotype PubMed 16899053. Source: MGI

   Cellular_componentcell periphery

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 14613966. Source: MGI

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 11884367. Source: MGI

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay Ref.8. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 11884367. Source: MGI

nucleus

Inferred from direct assay PubMed 14613966. Source: MGI

perinuclear region of cytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function14-3-3 protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin monomer binding

Inferred from direct assay Ref.4. Source: UniProtKB

calcium-independent protein kinase C activity

Inferred from direct assay PubMed 10879655. Source: MGI

enzyme activator activity

Inferred from electronic annotation. Source: Ensembl

ethanol binding

Inferred from direct assay PubMed 19432558. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay PubMed 17875639. Source: MGI

receptor activator activity

Inferred from direct assay PubMed 17875639. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YwhabQ9CQV86EBI-298451,EBI-771608

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 737737Protein kinase C epsilon type
PRO_0000055698

Regions

Domain1 – 9999C2
Domain408 – 668261Protein kinase
Domain669 – 73769AGC-kinase C-terminal
Zinc finger169 – 22052Phorbol-ester/DAG-type 1
Zinc finger242 – 29251Phorbol-ester/DAG-type 2
Nucleotide binding414 – 4229ATP By similarity
Motif223 – 2286Interaction with actin

Sites

Active site5321Proton acceptor By similarity
Binding site4371ATP By similarity

Amino acid modifications

Modified residue2281Phosphothreonine By similarity
Modified residue2341Phosphoserine Ref.12
Modified residue3091Phosphothreonine By similarity
Modified residue3161Phosphoserine Ref.12
Modified residue3291Phosphoserine By similarity
Modified residue3461Phosphoserine; by GSK3-beta Ref.13
Modified residue3501Phosphoserine; by MAPK11 and MAPK14 Ref.13
Modified residue3681Phosphoserine; by autocatalysis Ref.12 Ref.13
Modified residue3881Phosphoserine By similarity
Modified residue5661Phosphothreonine; by PDPK1 By similarity
Modified residue7031Phosphothreonine; by autocatalysis Potential
Modified residue7101Phosphothreonine; alternate Ref.6
Modified residue7101Phosphothreonine; by autocatalysis; alternate Potential
Modified residue7291Phosphoserine; by autocatalysis Probable

Experimental info

Mutagenesis3461S → A: Loss of interaction with YWHAB and defects in the completion of cytokinesis. Ref.13
Mutagenesis3681S → A: Loss of interaction with YWHAB and defects in the completion of cytokinesis. Ref.13
Mutagenesis7291S → A, E or T: Loss of localization to the perinuclear region. Loss of translocation to the nucleus upon PMA stimulation. Ref.11

Sequences

Sequence LengthMass (Da)Tools
P16054 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 7AEBB8CC10C99F57

FASTA73783,561
        10         20         30         40         50         60 
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT 

        70         80         90        100        110        120 
NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE 

       130        140        150        160        170        180 
PEGKVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP 

       190        200        210        220        230        240 
TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN 

       250        260        270        280        290        300 
MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA 

       310        320        330        340        350        360 
KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS PCDQELKELE 

       370        380        390        400        410        420 
NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA KRLGLDEFNF IKVLGKGSFG 

       430        440        450        460        470        480 
KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD 

       490        500        510        520        530        540 
RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL 

       550        560        570        580        590        600 
DAEGHCKLAD FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM 

       610        620        630        640        650        660 
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVAAQNGED 

       670        680        690        700        710        720 
AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPILT LVDEAIIKQI 

       730 
NQEEFKGFSY FGEDLMP 

« Hide

References

« Hide 'large scale' references
[1]"Unique substrate specificity and regulatory properties of PKC-epsilon: a rationale for diversity."
Schaap D., Parker P.J., Bristol A., Kriz R., Knopf J.
FEBS Lett. 243:351-357(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The catalytic domain of PKC-epsilon, in reciprocal PKC-delta and - epsilon chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-epsilon contribute to in vitro transformation."
Wang Q.J., Acs P., Goodnight J., Blumberg P.M., Mischak H., Mushinski J.F.
Oncogene 16:53-60(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]Wheeler D.L.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[4]"Biochemical and morphogenic effects of the interaction between protein kinase C-epsilon and actin in vitro and in cultured NIH3T3 cells."
Hernandez R.M., Wescott G.G., Mayhew M.W., McJilton M.A., Terrian D.M.
J. Cell. Biochem. 83:532-546(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ACTIN, ACTIN-BINDING MOTIF.
[5]"Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain."
Waldron R.T., Rozengurt E.
J. Biol. Chem. 278:154-163(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PRKD1.
[6]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[7]"Protein kinase C epsilon mediates angiotensin II-induced activation of beta1-integrins in cardiac fibroblasts."
Stawowy P., Margeta C., Blaschke F., Lindschau C., Spencer-Haensch C., Leitges M., Biagini G., Fleck E., Graf K.
Cardiovasc. Res. 67:50-59(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility."
Ivaska J., Vuoriluoto K., Huovinen T., Izawa I., Inagaki M., Parker P.J.
EMBO J. 24:3834-3845(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF VIM.
[9]"Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation."
Scruggs S.B., Walker L.A., Lyu T., Geenen D.L., Solaro R.J., Buttrick P.M., Goldspink P.H.
J. Mol. Cell. Cardiol. 40:465-473(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TNNI3.
[10]"Trif-related adapter molecule is phosphorylated by PKCepsilon during Toll-like receptor 4 signaling."
McGettrick A.F., Brint E.K., Palsson-McDermott E.M., Rowe D.C., Golenbock D.T., Gay N.J., Fitzgerald K.A., O'Neill L.A.J.
Proc. Natl. Acad. Sci. U.S.A. 103:9196-9201(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TICAM2/TRAM.
[11]"Phosphorylation at Ser729 specifies a Golgi localisation for protein kinase C epsilon (PKCepsilon) in 3T3 fibroblasts."
Xu T.R., He G., Dobson K., England K., Rumsby M.
Cell. Signal. 19:1986-1995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-729, MUTAGENESIS OF SER-729.
[12]"The identification and characterization of novel PKCepsilon phosphorylation sites provide evidence for functional cross-talk within the PKC superfamily."
Durgan J., Cameron A.J., Saurin A.T., Hanrahan S., Totty N., Messing R.O., Parker P.J.
Biochem. J. 411:319-331(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-234; SER-316 AND SER-368.
[13]"The regulated assembly of a PKCepsilon complex controls the completion of cytokinesis."
Saurin A.T., Durgan J., Cameron A.J., Faisal A., Marber M.S., Parker P.J.
Nat. Cell Biol. 10:891-901(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT SER-346; SER-350 AND SER-368, MUTAGENESIS OF SER-346 AND SER-368.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF028009 mRNA. Translation: AAB84189.1.
AF325507 mRNA. Translation: AAG53692.1.
CCDSCCDS29008.1.
PIRKIMSCE. S02270.
RefSeqNP_035234.1. NM_011104.3.
UniGeneMm.24614.

3D structure databases

ProteinModelPortalP16054.
SMRP16054. Positions 1-136, 168-736.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202198. 7 interactions.
DIPDIP-31066N.
IntActP16054. 92 interactions.
MINTMINT-98243.

Chemistry

BindingDBP16054.
ChEMBLCHEMBL4366.

PTM databases

PhosphoSiteP16054.

Proteomic databases

MaxQBP16054.
PaxDbP16054.
PRIDEP16054.

Protocols and materials databases

DNASU18754.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097274; ENSMUSP00000094873; ENSMUSG00000045038.
ENSMUST00000097275; ENSMUSP00000094874; ENSMUSG00000045038.
GeneID18754.
KEGGmmu:18754.
UCSCuc008dug.2. mouse.

Organism-specific databases

CTD5581.
MGIMGI:97599. Prkce.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117682.
HOGENOMHOG000233022.
HOVERGENHBG108317.
InParanoidP16054.
KOK18050.
OMAVANCNIS.
OrthoDBEOG77M8QM.
PhylomeDBP16054.
TreeFamTF351133.

Enzyme and pathway databases

BRENDA2.7.11.13. 3474.

Gene expression databases

ArrayExpressP16054.
BgeeP16054.
CleanExMM_PRKCE.
GenevestigatorP16054.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR027274. PKC_epsilon.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000551. PKC_delta. 1 hit.
PIRSF501106. Protein_kin_C_epsilon. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKCE. mouse.
NextBio294933.
PROP16054.
SOURCESearch...

Entry information

Entry nameKPCE_MOUSE
AccessionPrimary (citable) accession number: P16054
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot