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P20444

- KPCA_MOUSE

UniProt

P20444 - KPCA_MOUSE

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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

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 kinase C activity Source: MGI
  4. protein serine/threonine kinase activity Source: MGI
  5. 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
Complete GO annotation...

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. mitochondrion Source: MGI
  5. neuronal cell body Source: MGI
  6. nucleus Source: MGI
  7. perinuclear region of cytoplasm Source: UniProtKB
  8. photoreceptor outer segment Source: MGI
  9. plasma membrane Source: MGI
Complete GO annotation...

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.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
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]
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

        10         20         30         40         50
MADVYPANDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC
60 70 80 90 100
SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS
110 120 130 140 150
KHKFKIHTYG SPTFCDHCGS LLYGLIHQGM KCDTCDMNVH KQCVINDPSL
160 170 180 190 200
CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA KNLIPMDPNG LSDPYVKLKL
210 220 230 240 250
IPDPKNESKQ KTKTIRSNLN PQWNESFTFK LKPSDKDRRL SVEIWDWDRT
260 270 280 290 300
TRNDFMGSLS FGVSELMKMP ASGWYKAHNQ EEGEYYNVPI PEGDEEGNME
310 320 330 340 350
LRQKFEKAKL GPVGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF
360 370 380 390 400
GKVMLADRKG TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL
410 420 430 440 450
TQLHSCFQTV DRLYFVMEYV NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG
460 470 480 490 500
LFFLHKRGII YRDLKLNNVM LNSEGHIKIA DFGMCKEHMM DGVTTRTFCG
510 520 530 540 550
TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG EDEDELFQSI
560 570 580 590 600
MEHNVSYPKS LSKEAVSICK GLMTKQPAKR LGCGPEGERD VREHAFFRRI
610 620 630 640 650
DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ
660 670
SDFEGFSYVN PQFVHPILQS AV
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.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
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 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 29, 2014
This is version 158 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