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P20444

- KPCA_MOUSE

UniProt

P20444 - KPCA_MOUSE

Protein

Protein kinase C alpha type

Gene

Prkca

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascades involving MAPK1/3 (ERK1/2) and RAP1GAP. Depending on the cell type, is involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation. In cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Depending on the cell type, exhibits anti-apoptotic function and protects cells from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, or mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity.By similarity

    Enzyme regulationi

    Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-497 (activation loop of the kinase domain), Thr-638 (turn motif) and Ser-657 (hydrophobic region), need to be phosphorylated for its full activation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi186 – 1861Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi187 – 1871Calcium 1By similarity
    Metal bindingi187 – 1871Calcium 2By similarity
    Metal bindingi193 – 1931Calcium 2By similarity
    Binding sitei195 – 1951Inositol phosphate groupBy similarity
    Binding sitei245 – 2451Inositol phosphate groupBy similarity
    Metal bindingi246 – 2461Calcium 1By similarity
    Metal bindingi246 – 2461Calcium 2By similarity
    Metal bindingi247 – 2471Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi248 – 2481Calcium 1By similarity
    Metal bindingi248 – 2481Calcium 2By similarity
    Metal bindingi248 – 2481Calcium 3By similarity
    Metal bindingi252 – 2521Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi254 – 2541Calcium 1By similarity
    Metal bindingi254 – 2541Calcium 3By similarity
    Binding sitei368 – 3681ATPPROSITE-ProRule annotation
    Active sitei463 – 4631Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri36 – 8651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri101 – 15151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi345 – 3539ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium-dependent protein kinase C activity Source: MGI
    3. protein binding Source: IntAct
    4. protein kinase C activity Source: MGI
    5. protein serine/threonine kinase activity Source: MGI
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. cellular calcium ion homeostasis Source: MGI
    4. cellular response to carbohydrate stimulus Source: MGI
    5. chondrocyte differentiation Source: MGI
    6. inactivation of MAPK activity Source: MGI
    7. induction of positive chemotaxis Source: MGI
    8. intrinsic apoptotic signaling pathway Source: MGI
    9. negative regulation of cell proliferation Source: MGI
    10. negative regulation of glial cell apoptotic process Source: UniProtKB
    11. negative regulation of glucose import Source: MGI
    12. negative regulation of insulin receptor signaling pathway Source: MGI
    13. negative regulation of protein kinase activity Source: MGI
    14. negative regulation of protein phosphorylation Source: MGI
    15. neutrophil chemotaxis Source: MGI
    16. peptidyl-serine autophosphorylation Source: MGI
    17. positive regulation of angiogenesis Source: UniProtKB
    18. positive regulation of cardiac muscle hypertrophy Source: UniProtKB
    19. positive regulation of cell adhesion Source: UniProtKB
    20. positive regulation of cell migration Source: UniProtKB
    21. positive regulation of dense core granule biogenesis Source: UniProtKB
    22. positive regulation of endothelial cell migration Source: UniProtKB
    23. positive regulation of endothelial cell proliferation Source: UniProtKB
    24. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    25. positive regulation of inflammatory response Source: MGI
    26. positive regulation of lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    27. positive regulation of macrophage differentiation Source: UniProtKB
    28. positive regulation of mitotic cell cycle Source: UniProtKB
    29. positive regulation of protein phosphorylation Source: MGI
    30. protein phosphorylation Source: MGI
    31. regulation of muscle contraction Source: MGI
    32. regulation of peptidyl-tyrosine phosphorylation Source: MGI
    33. regulation of platelet aggregation Source: UniProtKB
    34. regulation of the force of heart contraction Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Cell adhesion

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C alpha type (EC:2.7.11.13)
    Short name:
    PKC-A
    Short name:
    PKC-alpha
    Gene namesi
    Name:Prkca
    Synonyms:Pkca
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:97595. Prkca.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein. Mitochondrion membrane Curated; Peripheral membrane protein Curated. Nucleus
    Note: Translocated to the cell periphery upon tetradecanoyl phorbol acetate (TPA) treatment.

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. cytoplasm Source: MGI
    3. dendrite Source: MGI
    4. mitochondrial membrane Source: UniProtKB-SubCell
    5. mitochondrion Source: MGI
    6. neuronal cell body Source: MGI
    7. nucleus Source: MGI
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. photoreceptor outer segment Source: MGI
    10. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Expression of the mutant form UV25 causes malignant transformation of cells.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 672671Protein kinase C alpha typePRO_0000055680Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei226 – 2261PhosphoserineBy similarity
    Modified residuei250 – 2501Phosphothreonine; by autocatalysisBy similarity
    Modified residuei497 – 4971Phosphothreonine; by PDPK1By similarity
    Modified residuei628 – 6281N6-acetyllysineBy similarity
    Modified residuei631 – 6311Phosphothreonine; by autocatalysisSequence Analysis
    Modified residuei638 – 6381Phosphothreonine; by autocatalysisBy similarity
    Modified residuei651 – 6511PhosphoserineBy similarity
    Modified residuei657 – 6571PhosphoserineBy similarity
    Modified residuei658 – 6581Phosphotyrosine; by SYK1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP20444.
    PaxDbiP20444.
    PRIDEiP20444.

    PTM databases

    PhosphoSiteiP20444.

    Expressioni

    Gene expression databases

    CleanExiMM_PRKCA.
    GenevestigatoriP20444.

    Interactioni

    Subunit structurei

    Interacts with ADAP1/CENTA1, CSPG4 and PRKCABP. Binds to SDPR in the presence of phosphatidylserine By similarity. Interacts with PICK1 (via PDZ domain) By similarity. Interacts with TRIM41 By similarity. Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and GNB2L1/RACK1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ClockO087853EBI-6976815,EBI-79859

    Protein-protein interaction databases

    BioGridi202194. 8 interactions.
    DIPiDIP-532N.
    IntActiP20444. 3 interactions.
    MINTiMINT-98140.

    Structurei

    3D structure databases

    ProteinModelPortaliP20444.
    SMRiP20444. Positions 37-670.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini172 – 26089C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 597259Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini598 – 66871AGC-kinase C-terminalAdd
    BLAST

    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 fingeri36 – 8651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri101 – 15151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233022.
    HOVERGENiHBG108317.
    InParanoidiP20444.
    KOiK02677.
    PhylomeDBiP20444.

    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.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014375. Protein_kinase_C_a/b/g.
    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]
    PIRSFiPIRSF000550. PKC_alpha. 1 hit.
    PRINTSiPR00360. C2DOMAIN.
    PR00008. 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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P20444-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADVYPANDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC    50
    SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS 100
    KHKFKIHTYG SPTFCDHCGS LLYGLIHQGM KCDTCDMNVH KQCVINDPSL 150
    CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA KNLIPMDPNG LSDPYVKLKL 200
    IPDPKNESKQ KTKTIRSNLN PQWNESFTFK LKPSDKDRRL SVEIWDWDRT 250
    TRNDFMGSLS FGVSELMKMP ASGWYKAHNQ EEGEYYNVPI PEGDEEGNME 300
    LRQKFEKAKL GPVGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF 350
    GKVMLADRKG TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL 400
    TQLHSCFQTV DRLYFVMEYV NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG 450
    LFFLHKRGII YRDLKLNNVM LNSEGHIKIA DFGMCKEHMM DGVTTRTFCG 500
    TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG EDEDELFQSI 550
    MEHNVSYPKS LSKEAVSICK GLMTKQPAKR LGCGPEGERD VREHAFFRRI 600
    DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ 650
    SDFEGFSYVN PQFVHPILQS AV 672
    Length:672
    Mass (Da):76,852
    Last modified:January 23, 2007 - v3
    Checksum:i394B48C952BB6D50
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471D → V in CAA36908. (PubMed:2469625)Curated
    Sequence conflicti147 – 1471D → V in CAA36907. (PubMed:2469625)Curated
    Sequence conflicti218 – 2181N → T in CAA36908. (PubMed:2469625)Curated
    Sequence conflicti218 – 2181N → T in CAA36907. (PubMed:2469625)Curated
    Sequence conflicti277 – 2782AH → LL in CAA36908. (PubMed:2469625)Curated
    Sequence conflicti277 – 2782AH → LL in CAA36907. (PubMed:2469625)Curated
    Sequence conflicti313 – 3131V → A in CAA36908. (PubMed:2469625)Curated
    Sequence conflicti313 – 3131V → A in CAA36907. (PubMed:2469625)Curated
    Sequence conflicti467 – 4671N → D in CAA36908. (PubMed:2469625)Curated
    Sequence conflicti467 – 4671N → D in CAA36907. (PubMed:2469625)Curated
    Sequence conflicti472 – 4721N → D in CAA36908. (PubMed:2469625)Curated
    Sequence conflicti472 – 4721N → D in CAA36907. (PubMed:2469625)Curated
    Sequence conflicti576 – 5761Q → H in CAA36908. (PubMed:2469625)Curated
    Sequence conflicti576 – 5761Q → H in CAA36907. (PubMed:2469625)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061I → V in mutant form UV25. 1 Publication
    Natural varianti111 – 1111S → G in mutant form UV25. 1 Publication
    Natural varianti240 – 2401L → Q in mutant form UV25. 1 Publication
    Natural varianti339 – 3391F → L in mutant form UV25. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25811 mRNA. Translation: AAA39934.1.
    X52685 mRNA. Translation: CAA36908.1.
    X52684 mRNA. Translation: CAA36907.1.
    PIRiS07104. KIMSCA.
    RefSeqiNP_035231.2. NM_011101.3.
    UniGeneiMm.222178.

    Genome annotation databases

    GeneIDi18750.
    KEGGimmu:18750.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25811 mRNA. Translation: AAA39934.1 .
    X52685 mRNA. Translation: CAA36908.1 .
    X52684 mRNA. Translation: CAA36907.1 .
    PIRi S07104. KIMSCA.
    RefSeqi NP_035231.2. NM_011101.3.
    UniGenei Mm.222178.

    3D structure databases

    ProteinModelPortali P20444.
    SMRi P20444. Positions 37-670.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202194. 8 interactions.
    DIPi DIP-532N.
    IntActi P20444. 3 interactions.
    MINTi MINT-98140.

    Chemistry

    BindingDBi P20444.
    ChEMBLi CHEMBL2567.

    PTM databases

    PhosphoSitei P20444.

    Proteomic databases

    MaxQBi P20444.
    PaxDbi P20444.
    PRIDEi P20444.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 18750.
    KEGGi mmu:18750.

    Organism-specific databases

    CTDi 5578.
    MGIi MGI:97595. Prkca.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233022.
    HOVERGENi HBG108317.
    InParanoidi P20444.
    KOi K02677.
    PhylomeDBi P20444.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 3474.

    Miscellaneous databases

    ChiTaRSi PRKCA. mouse.
    NextBioi 294917.
    PROi P20444.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_PRKCA.
    Genevestigatori P20444.

    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.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014375. Protein_kinase_C_a/b/g.
    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 PIRSF000550. PKC_alpha. 1 hit.
    PRINTSi PR00360. C2DOMAIN.
    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. "Molecular cloning of mouse protein kinase C (PKC) cDNA from Swiss 3T3 fibroblasts."
      Rose-John S., Dietrich A., Marks F.
      Gene 74:465-471(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A mutant protein kinase C that can transform fibroblasts."
      Megidish T., Mazurek N.
      Nature 342:807-811(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-106; GLY-111; GLN-240 AND LEU-339.
      Strain: BALB/c.
      Tissue: Brain.
    3. "Protein kinase C alpha activates RAF-1 by direct phosphorylation."
      Kolch W., Heidecker G., Kochs G., Hummel R., Vahidi H., Mischak H., Finkenzeller G., Marme D., Rapp U.R.
      Nature 364:249-252(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RAF1.
    4. "PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system."
      Staudinger J., Zhou J., Burgess R., Elledge S.J., Olson E.N.
      J. Cell Biol. 128:263-271(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCABP.
    5. "An activated protein kinase C alpha gives a differentiation signal for hematopoietic progenitor cells and mimicks macrophage colony-stimulating factor-stimulated signaling events."
      Pierce A., Heyworth C.M., Nicholls S.E., Spooncer E., Dexter T.M., Lord J.M., Owen-Lynch P.J., Wark G., Whetton A.D.
      J. Cell Biol. 140:1511-1518(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL PROLIFERATION.
    6. Cited for: SUBCELLULAR LOCATION.
    7. Cited for: PHOSPHORYLATION AT TYR-658.
    8. Cited for: FUNCTION IN PLATELET GRANULE SECRETION.
    9. "Identification of RACK1 and protein kinase Calpha as integral components of the mammalian circadian clock."
      Robles M.S., Boyault C., Knutti D., Padmanabhan K., Weitz C.J.
      Science 327:463-466(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BMAL1 AND GNB2L1, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiKPCA_MOUSE
    AccessioniPrimary (citable) accession number: P20444
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3