Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein kinase C alpha type (PKC-A) (PKC-alpha) (EC 2.7.11.13)

 KPCA_MOUSE              Reviewed;         672 AA.
P20444;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 184.
RecName: Full=Protein kinase C alpha type;
Short=PKC-A;
Short=PKC-alpha;
EC=2.7.11.13;
Name=Prkca; Synonyms=Pkca;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2469625; DOI=10.1016/0378-1119(88)90179-5;
Rose-John S., Dietrich A., Marks F.;
"Molecular cloning of mouse protein kinase C (PKC) cDNA from Swiss 3T3
fibroblasts.";
Gene 74:465-471(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-106; GLY-111; GLN-240 AND
LEU-339.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=2601739; DOI=10.1038/342807a0;
Megidish T., Mazurek N.;
"A mutant protein kinase C that can transform fibroblasts.";
Nature 342:807-811(1989).
[3]
FUNCTION IN PHOSPHORYLATION OF RAF1.
PubMed=8321321; DOI=10.1038/364249a0;
Kolch W., Heidecker G., Kochs G., Hummel R., Vahidi H., Mischak H.,
Finkenzeller G., Marme D., Rapp U.R.;
"Protein kinase C alpha activates RAF-1 by direct phosphorylation.";
Nature 364:249-252(1993).
[4]
INTERACTION WITH PRKCABP.
PubMed=7844141; DOI=10.1083/jcb.128.3.263;
Staudinger J., Zhou J., Burgess R., Elledge S.J., Olson E.N.;
"PICK1: a perinuclear binding protein and substrate for protein kinase
C isolated by the yeast two-hybrid system.";
J. Cell Biol. 128:263-271(1995).
[5]
FUNCTION IN CELL PROLIFERATION.
PubMed=9508782; DOI=10.1083/jcb.140.6.1511;
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.;
"An activated protein kinase C alpha gives a differentiation signal
for hematopoietic progenitor cells and mimicks macrophage colony-
stimulating factor-stimulated signaling events.";
J. Cell Biol. 140:1511-1518(1998).
[6]
SUBCELLULAR LOCATION.
PubMed=10092232; DOI=10.1126/science.283.5410.2085;
Ng T., Squire A., Hansra G., Bornancin F., Prevostel C., Hanby A.,
Harris W., Barnes D., Schmidt S., Mellor H., Bastiaens P.I.,
Parker P.J.;
"Imaging protein kinase Calpha activation in cells.";
Science 283:2085-2089(1999).
[7]
PHOSPHORYLATION AT TYR-658.
PubMed=12881490; DOI=10.1073/pnas.1633695100;
Kawakami Y., Kitaura J., Yao L., McHenry R.W., Kawakami Y.,
Newton A.C., Kang S., Kato R.M., Leitges M., Rawlings D.J.,
Kawakami T.;
"A Ras activation pathway dependent on Syk phosphorylation of protein
kinase C.";
Proc. Natl. Acad. Sci. U.S.A. 100:9470-9475(2003).
[8]
FUNCTION IN PLATELET GRANULE SECRETION.
PubMed=19147982; DOI=10.1172/JCI34665;
Konopatskaya O., Gilio K., Harper M.T., Zhao Y., Cosemans J.M.,
Karim Z.A., Whiteheart S.W., Molkentin J.D., Verkade P., Watson S.P.,
Heemskerk J.W., Poole A.W.;
"PKCalpha regulates platelet granule secretion and thrombus formation
in mice.";
J. Clin. Invest. 119:399-407(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
INTERACTION WITH BMAL1 AND RACK1, AND SUBCELLULAR LOCATION.
PubMed=20093473; DOI=10.1126/science.1180067;
Robles M.S., Boyault C., Knutti D., Padmanabhan K., Weitz C.J.;
"Identification of RACK1 and protein kinase Calpha as integral
components of the mammalian circadian clock.";
Science 327:463-466(2010).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:19147982, ECO:0000269|PubMed:8321321,
ECO:0000269|PubMed:9508782}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P05696};
Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
domain. {ECO:0000250|UniProtKB:P05696};
-!- ENZYME REGULATION: 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.
-!- SUBUNIT: Interacts with ADAP1/CENTA1 and CSPG4 (By
similarity).Interacts with PRKCABP (PubMed:7844141). Binds to
CAVIN2 in the presence of phosphatidylserine. Interacts with PICK1
(via PDZ domain). Interacts with TRIM41 (By similarity). Recruited
in a circadian manner into a nuclear complex which also includes
BMAL1 and RACK1 (PubMed:20093473). {ECO:0000250|UniProtKB:P05696,
ECO:0000250|UniProtKB:P17252, ECO:0000269|PubMed:20093473,
ECO:0000269|PubMed:7844141}.
-!- INTERACTION:
O08785:Clock; NbExp=3; IntAct=EBI-6976815, EBI-79859;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10092232,
ECO:0000269|PubMed:20093473}. Cell membrane
{ECO:0000269|PubMed:10092232}; Peripheral membrane protein
{ECO:0000305|PubMed:10092232}. Mitochondrion membrane
{ECO:0000250|UniProtKB:P17252}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P17252}. Nucleus
{ECO:0000269|PubMed:20093473}. Note=Translocated to the cell
periphery upon tetradecanoyl phorbol acetate (TPA) treatment.
-!- DISEASE: Note=Expression of the mutant form UV25 causes malignant
transformation of cells.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M25811; AAA39934.1; -; mRNA.
EMBL; X52685; CAA36908.1; -; mRNA.
EMBL; X52684; CAA36907.1; -; mRNA.
PIR; S07104; KIMSCA.
RefSeq; NP_035231.2; NM_011101.3.
UniGene; Mm.222178; -.
DisProt; DP01105; -.
ProteinModelPortal; P20444; -.
SMR; P20444; -.
BioGrid; 202194; 10.
DIP; DIP-532N; -.
IntAct; P20444; 3.
MINT; MINT-98140; -.
STRING; 10090.ENSMUSP00000062392; -.
BindingDB; P20444; -.
ChEMBL; CHEMBL2567; -.
iPTMnet; P20444; -.
PhosphoSitePlus; P20444; -.
EPD; P20444; -.
MaxQB; P20444; -.
PaxDb; P20444; -.
PeptideAtlas; P20444; -.
PRIDE; P20444; -.
GeneID; 18750; -.
KEGG; mmu:18750; -.
CTD; 5578; -.
MGI; MGI:97595; Prkca.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P20444; -.
KO; K02677; -.
PhylomeDB; P20444; -.
BRENDA; 2.7.11.13; 3474.
ChiTaRS; Prkca; mouse.
PRO; PR:P20444; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PRKCA; -.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004698; F:calcium-dependent protein kinase C activity; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0035403; F:histone kinase activity (H3-T6 specific); ISO:MGI.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0004697; F:protein kinase C activity; IDA:CACAO.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
GO; GO:0071322; P:cellular response to carbohydrate stimulus; IDA:MGI.
GO; GO:0002062; P:chondrocyte differentiation; IDA:MGI.
GO; GO:0002159; P:desmosome assembly; ISO:MGI.
GO; GO:0035408; P:histone H3-T6 phosphorylation; ISO:MGI.
GO; GO:0000188; P:inactivation of MAPK activity; IMP:MGI.
GO; GO:0050930; P:induction of positive chemotaxis; IMP:MGI.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0010360; P:negative regulation of anion channel activity; IMP:CAFA.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
GO; GO:0046325; P:negative regulation of glucose import; IMP:MGI.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI.
GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
GO; GO:0036289; P:peptidyl-serine autophosphorylation; IDA:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:2000707; P:positive regulation of dense core granule biogenesis; IMP:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IMP:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0006937; P:regulation of muscle contraction; IMP:MGI.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0090330; P:regulation of platelet aggregation; IMP:UniProtKB.
GO; GO:0047484; P:regulation of response to osmotic stress; IMP:CAFA.
GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
CDD; cd00029; C1; 2.
CDD; cd05615; STKc_cPKC_alpha; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR034663; cPKC_alpha.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR014375; Protein_kinase_C_a/b/g.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00168; C2; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000550; PKC_alpha; 1.
PRINTS; PR00360; C2DOMAIN.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00239; C2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
1: Evidence at protein level;
Acetylation; Angiogenesis; Apoptosis; ATP-binding; Calcium;
Cell adhesion; Cell membrane; Complete proteome; Cytoplasm; Kinase;
Membrane; Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P17252}.
CHAIN 2 672 Protein kinase C alpha type.
/FTId=PRO_0000055680.
DOMAIN 172 260 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 339 597 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 598 668 AGC-kinase C-terminal.
ZN_FING 36 86 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 101 151 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 345 353 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 463 463 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 186 186 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 187 187 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 187 187 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 193 193 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 246 246 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 246 246 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 247 247 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 2.
{ECO:0000250|UniProtKB:P05696}.
METAL 248 248 Calcium 3.
{ECO:0000250|UniProtKB:P05696}.
METAL 252 252 Calcium 3; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P05696}.
METAL 254 254 Calcium 1.
{ECO:0000250|UniProtKB:P05696}.
METAL 254 254 Calcium 3.
{ECO:0000250|UniProtKB:P05696}.
BINDING 195 195 Inositol phosphate group.
{ECO:0000250|UniProtKB:P05696}.
BINDING 245 245 Inositol phosphate group.
{ECO:0000250|UniProtKB:P05696}.
BINDING 368 368 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000250|UniProtKB:P05696}.
MOD_RES 497 497 Phosphothreonine; by PDPK1.
{ECO:0000250}.
MOD_RES 501 501 Phosphothreonine.
{ECO:0000250|UniProtKB:P05771}.
MOD_RES 628 628 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 631 631 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P68403,
ECO:0000255}.
MOD_RES 638 638 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:P17252}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000250|UniProtKB:P05771}.
MOD_RES 658 658 Phosphotyrosine; by SYK.
{ECO:0000269|PubMed:12881490}.
VARIANT 106 106 I -> V (in mutant form UV25).
{ECO:0000269|PubMed:2601739}.
VARIANT 111 111 S -> G (in mutant form UV25).
{ECO:0000269|PubMed:2601739}.
VARIANT 240 240 L -> Q (in mutant form UV25).
{ECO:0000269|PubMed:2601739}.
VARIANT 339 339 F -> L (in mutant form UV25).
{ECO:0000269|PubMed:2601739}.
CONFLICT 147 147 D -> V (in Ref. 1; CAA36908/CAA36907).
{ECO:0000305}.
CONFLICT 218 218 N -> T (in Ref. 1; CAA36908/CAA36907).
{ECO:0000305}.
CONFLICT 277 278 AH -> LL (in Ref. 1; CAA36908/CAA36907).
{ECO:0000305}.
CONFLICT 313 313 V -> A (in Ref. 1; CAA36908/CAA36907).
{ECO:0000305}.
CONFLICT 467 467 N -> D (in Ref. 1; CAA36908/CAA36907).
{ECO:0000305}.
CONFLICT 472 472 N -> D (in Ref. 1; CAA36908/CAA36907).
{ECO:0000305}.
CONFLICT 576 576 Q -> H (in Ref. 1; CAA36908/CAA36907).
{ECO:0000305}.
SEQUENCE 672 AA; 76852 MW; 394B48C952BB6D50 CRC64;
MADVYPANDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC SHCTDFIWGF
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS KHKFKIHTYG SPTFCDHCGS
LLYGLIHQGM KCDTCDMNVH KQCVINDPSL CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA
KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSNLN PQWNESFTFK LKPSDKDRRL
SVEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKAHNQ EEGEYYNVPI PEGDEEGNME
LRQKFEKAKL GPVGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF GKVMLADRKG
TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL TQLHSCFQTV DRLYFVMEYV
NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG LFFLHKRGII YRDLKLNNVM LNSEGHIKIA
DFGMCKEHMM DGVTTRTFCG TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG
EDEDELFQSI MEHNVSYPKS LSKEAVSICK GLMTKQPAKR LGCGPEGERD VREHAFFRRI
DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ SDFEGFSYVN
PQFVHPILQS AV


Related products :

Catalog number Product name Quantity
17-662-20008 Calcium_calmodulin-dependent protein kinase type II alpha chain - EC 2.7.11.17; CaM-kinase II alpha chain; CaM kinase II alpha subunit; CaMK-II subunit alpha Serum 0.1 ml
18-662-20052 Calcium_calmodulin-dependent protein kinase type II alpha chain - EC 2.7.11.17; CaM-kinase II alpha chain; CaM kinase II alpha subunit; CaMK-II subunit alpha Polyclonal 0.1 ml
E0655h ELISA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,CAMK2A,CAMKA,CaMK-II subunit alpha,Homo sapiens,Human,KIAA0968 96T
U0655h CLIA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,CAMK2A,CAMKA,CaMK-II subunit alpha,Homo sapiens,Human,KIAA0968 96T
E0655h ELISA kit Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,CAMK2A,CAMKA,CaMK-II subunit alpha,Homo sapiens,Human,KIAA0968 96T
E0655r ELISA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Rat,Rattus norvegicus 96T
E0655m ELISA kit Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Mouse,Mus musculus 96T
E0655m ELISA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Mouse,Mus musculus 96T
U0655r CLIA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Rat,Rattus norvegicus 96T
E0655r ELISA kit Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Rat,Rattus norvegicus 96T
U0655m CLIA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Mouse,Mus musculus 96T
orb80847 Protein Kinase Inactive holoenzyme type alpha protein Inactive holoenzyme consisting of one dimeric regulatory subunit type alpha and two monomeric catalytic subunits (cAMP-free). Protein Kinase Recom 1
orb80848 Protein Kinase Inactive holoenzyme type alpha protein Inactive holoenzyme consisting of one dimeric regulatory subunit type II alpha and two monomeric catalytic subunits (cAMP-free). Protein Kinase is 1
EIAAB31006 Homo sapiens,Human,Phosphatidylinositol 4-kinase alpha,PI4KA,PI4K-alpha,PI4-kinase alpha,PIK4,PIK4CA,PtdIns-4-kinase alpha
EIAAB25359 CDC42-binding protein kinase alpha,CDC42BPA,DMPK-like alpha,Homo sapiens,Human,KIAA0451,MRCK alpha,Myotonic dystrophy kinase-related CDC42-binding kinase alpha,Myotonic dystrophy protein kinase-like a
EIAAB31007 Bos taurus,Bovine,Phosphatidylinositol 4-kinase alpha,PI4KA,PI4K-alpha,PI4-kinase alpha,PIK4CA,PtdIns-4-kinase alpha
18-785-210338 p70 S6 Kinase (Phospho-Ser411) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-785-210338 p70 S6 Kinase (Phospho-Ser411) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210337 p70 S6 Kinase (Phospho-Thr421) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-785-210337 p70 S6 Kinase (Phospho-Thr421) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
18-785-210339 p70 S6 Kinase (Phospho-Ser424) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.05 mg
18-785-210339 p70 S6 Kinase (Phospho-Ser424) - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha Polyclonal 0.1 mg
SCH-MCA1572 MOUSE ANTI PROTEIN KINASE C ALPHA, Product Type Monoclonal Antibody, Specificity PROTEIN KINASE C ALPHA, Target Species , Host Mouse, Format S_N, Isotypes IgG2a, Applications C, WB, Clone 133 2 ml
MCA1572 MOUSE ANTI PROTEIN KINASE C ALPHA, Product Type Monoclonal Antibody, Specificity PROTEIN KINASE C ALPHA, Target Species , Host Mouse, Format S_N, Isotypes IgG2a, Applications C, WB, Clone 133 2 ml
EIAAB25358 CDC42-binding protein kinase alpha,Cdc42bpa,MRCK alpha,Myotonic dystrophy kinase-related CDC42-binding kinase alpha,Myotonic dystrophy protein kinase-like alpha,Pk428,Rat,Rattus norvegicus,Serine_thre


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur