KPCB_MOUSE
ID KPCB_MOUSE Reviewed; 671 AA.
AC P68404; A0JNZ5; F2Z441; P04410; P04411;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein kinase C beta type;
DE Short=PKC-B;
DE Short=PKC-beta;
DE EC=2.7.11.13;
GN Name=Prkcb; Synonyms=Pkcb, Prkcb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-I).
RC STRAIN=ICR X Swiss Webster; TISSUE=Brain;
RX PubMed=2402470; DOI=10.1093/nar/18.17.5310;
RA Tang Y.-M., Ashendel C.L.;
RT "Isolation of cloned mouse protein kinase C beta-II cDNA and its
RT sequence.";
RL Nucleic Acids Res. 18:5310-5310(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II).
RA Powell C.T.;
RT "Nucleotide sequence of cDNA for mouse brain protein kinase C beta-I
RT subspecies.";
RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BETA-I).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8670417; DOI=10.1126/science.273.5276.788;
RA Leitges M., Schmedt C., Guinamard R., Davoust J., Schaal S., Stabel S.,
RA Tarakhovsky A.;
RT "Immunodeficiency in protein kinase cbeta-deficient mice.";
RL Science 273:788-791(1996).
RN [6]
RP FUNCTION IN INSULIN SIGNALING.
RX PubMed=10499500; DOI=10.1210/endo.140.10.7073;
RA Standaert M.L., Bandyopadhyay G., Galloway L., Soto J., Ono Y., Kikkawa U.,
RA Farese R.V., Leitges M.;
RT "Effects of knockout of the protein kinase C beta gene on glucose transport
RT and glucose homeostasis.";
RL Endocrinology 140:4470-4477(1999).
RN [7]
RP FUNCTION.
RX PubMed=12070292; DOI=10.1084/jem.20020408;
RA Saijo K., Mecklenbrauker I., Santana A., Leitger M., Schmedt C.,
RA Tarakhovsky A.;
RT "Protein kinase C beta controls nuclear factor kappaB activation in B cells
RT through selective regulation of the IkappaB kinase alpha.";
RL J. Exp. Med. 195:1647-1652(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12118249; DOI=10.1038/ni823;
RA Su T.T., Guo B., Kawakami Y., Sommer K., Chae K., Humphries L.A.,
RA Kato R.M., Kang S., Patrone L., Wall R., Teitell M., Leitges M.,
RA Kawakami T., Rawlings D.J.;
RT "PKC-beta controls I kappa B kinase lipid raft recruitment and activation
RT in response to BCR signaling.";
RL Nat. Immunol. 3:780-786(2002).
RN [9]
RP FUNCTION IN ENDOTHELIAL CELLS PROLIFERATION.
RX PubMed=11805327; DOI=10.1073/pnas.022644499;
RA Suzuma K., Takahara N., Suzuma I., Isshiki K., Ueki K., Leitges M.,
RA Aiello L.P., King G.L.;
RT "Characterization of protein kinase C beta isoform's action on
RT retinoblastoma protein phosphorylation, vascular endothelial growth factor-
RT induced endothelial cell proliferation, and retinal neovascularization.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:721-726(2002).
RN [10]
RP PHOSPHORYLATION AT TYR-662.
RX PubMed=12881490; DOI=10.1073/pnas.1633695100;
RA Kawakami Y., Kitaura J., Yao L., McHenry R.W., Kawakami Y., Newton A.C.,
RA Kang S., Kato R.M., Leitges M., Rawlings D.J., Kawakami T.;
RT "A Ras activation pathway dependent on Syk phosphorylation of protein
RT kinase C.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9470-9475(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH CARD11.
RX PubMed=16356855; DOI=10.1016/j.immuni.2005.09.014;
RA Sommer K., Guo B., Pomerantz J.L., Bandaranayake A.D., Moreno-Garcia M.E.,
RA Ovechkina Y.L., Rawlings D.J.;
RT "Phosphorylation of the CARMA1 linker controls NF-kappaB activation.";
RL Immunity 23:561-574(2005).
RN [12]
RP FUNCTION IN NF-KAPPA-B ACTIVATION.
RX PubMed=16301747; DOI=10.1084/jem.20051591;
RA Shinohara H., Yasuda T., Aiba Y., Sanjo H., Hamadate M., Watarai H.,
RA Sakurai H., Kurosaki T.;
RT "PKC beta regulates BCR-mediated IKK activation by facilitating the
RT interaction between TAK1 and CARMA1.";
RL J. Exp. Med. 202:1423-1431(2005).
RN [13]
RP FUNCTION IN ENDOTHELIAL CELLS.
RX PubMed=16505232; DOI=10.2337/diabetes.55.03.06.db05-0771;
RA Naruse K., Rask-Madsen C., Takahara N., Ha S.W., Suzuma K., Way K.J.,
RA Jacobs J.R., Clermont A.C., Ueki K., Ohshiro Y., Zhang J., Goldfine A.B.,
RA King G.L.;
RT "Activation of vascular protein kinase C-beta inhibits Akt-dependent
RT endothelial nitric oxide synthase function in obesity-associated insulin
RT resistance.";
RL Diabetes 55:691-698(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641 (ISOFORM BETA-II), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [16]
RP FUNCTION.
RX PubMed=17272725; DOI=10.1126/science.1135380;
RA Pinton P., Rimessi A., Marchi S., Orsini F., Migliaccio E., Giorgio M.,
RA Contursi C., Minucci S., Mantovani F., Wieckowski M.R., Del Sal G.,
RA Pelicci P.G., Rizzuto R.;
RT "Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial
RT effects of the life-span determinant p66Shc.";
RL Science 315:659-663(2007).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=17962198; DOI=10.1074/jbc.m707268200;
RA Bansode R.R., Huang W., Roy S.K., Mehta M., Mehta K.D.;
RT "Protein kinase C deficiency increases fatty acid oxidation and reduces fat
RT storage.";
RL J. Biol. Chem. 283:231-236(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641; SER-654; SER-660;
RP SER-664 AND SER-673 (ISOFORM BETA-II), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-
CC dependent serine/threonine-protein kinase involved in various cellular
CC processes such as regulation of the B-cell receptor (BCR) signalosome,
CC oxidative stress-induced apoptosis, androgen receptor-dependent
CC transcription regulation, insulin signaling and endothelial cells
CC proliferation. Plays a key role in B-cell activation by regulating BCR-
CC induced NF-kappa-B activation. Mediates the activation of the canonical
CC NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1
CC at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces
CC CARD11/CARMA1 association with lipid rafts and recruitment of the
CC BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK
CC complex, resulting in nuclear translocation and activation of NFKB1.
CC Plays a direct role in the negative feedback regulation of the BCR
CC signaling, by down-modulating BTK function via direct phosphorylation
CC of BTK at 'Ser-180', which results in the alteration of BTK plasma
CC membrane localization and in turn inhibition of BTK activity. Involved
CC in apoptosis following oxidative damage: in case of oxidative
CC conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of
CC SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc
CC acts as a reactive oxygen species producer. Acts as a coactivator of
CC androgen receptor (ANDR)-dependent transcription, by being recruited to
CC ANDR target genes and specifically mediating phosphorylation of 'Thr-6'
CC of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional
CC activation that prevents demethylation of histone H3 'Lys-4' (H3K4me)
CC by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in
CC muscle cells and mediate insulin-dependent DNA synthesis through the
CC RAF1-MAPK/ERK signaling cascade. Participates in the regulation of
CC glucose transport in adipocytes by negatively modulating the insulin-
CC stimulated translocation of the glucose transporter SLC2A4/GLUT4.
CC Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1.
CC Under high glucose in pancreatic beta-cells, is probably involved in
CC the inhibition of the insulin gene transcription, via regulation of MYC
CC expression. In endothelial cells, activation of PRKCB induces increased
CC phosphorylation of RB1, increased VEGFA-induced cell proliferation, and
CC inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS)
CC regulation by insulin, which causes endothelial dysfunction. Also
CC involved in triglyceride homeostasis. Phosphorylates ATF2 which
CC promotes cooperation between ATF2 and JUN, activating transcription (By
CC similarity). {ECO:0000250|UniProtKB:P05771,
CC ECO:0000269|PubMed:10499500, ECO:0000269|PubMed:11805327,
CC ECO:0000269|PubMed:12070292, ECO:0000269|PubMed:12118249,
CC ECO:0000269|PubMed:16301747, ECO:0000269|PubMed:16356855,
CC ECO:0000269|PubMed:16505232, ECO:0000269|PubMed:17272725,
CC ECO:0000269|PubMed:8670417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domain. {ECO:0000250|UniProtKB:P68403};
CC -!- ACTIVITY REGULATION: Classical (or conventional) PKCs (PRKCA, PRKCB and
CC PRKCG) are activated by calcium and diacylglycerol (DAG) in the
CC presence of phosphatidylserine. Three specific sites; Thr-500
CC (activation loop of the kinase domain), Thr-642 (turn motif) and Ser-
CC 661 (hydrophobic region), need to be phosphorylated for its full
CC activation. Specifically inhibited by enzastaurin (LY317615) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PDK1. Interacts in vitro with PRKCBP1.
CC Interacts with PHLPP1 and PHLPP2; both proteins mediate its
CC dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and ANDR (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P68404; Q13873: BMPR2; Xeno; NbExp=4; IntAct=EBI-397048, EBI-527196;
CC P68404; P56537: EIF6; Xeno; NbExp=2; IntAct=EBI-397048, EBI-372243;
CC P68404-2; P48736: PIK3CG; Xeno; NbExp=2; IntAct=EBI-16063464, EBI-1030384;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta-I;
CC IsoId=P68404-1; Sequence=Displayed;
CC Name=Beta-II;
CC IsoId=P68404-2; Sequence=VSP_041812;
CC -!- PTM: Phosphorylation on Thr-500 within the activation loop renders it
CC competent to autophosphorylate. Subsequent autophosphorylation of Thr-
CC 642 maintains catalytic competence, and autophosphorylation on Ser-661
CC appears to release the kinase into the cytosol. Autophosphorylation on
CC other sites i.e. in the N-terminal and hinge regions have no effect on
CC enzyme activity (By similarity). Phosphorylation at Tyr-662 by SYK
CC induces binding with GRB2 and contributes to the activation of MAPK/ERK
CC signaling cascade. {ECO:0000250, ECO:0000269|PubMed:12881490}.
CC -!- DISRUPTION PHENOTYPE: Mice develop an immunodeficiency characterized by
CC impaired humoral immune responses and reduced cellular responses of B-
CC cells similar to X-linked immunodeficiency (Xid). Mice are unable to
CC activate NF-kappa-B and promote cell survival in B-cells upon BCR
CC signaling, or even in mast cells. B-cells fail to recruit the I-kappa-B
CC kinase (IKK) complex into lipid rafts, activate IKK, degrade I-kappa-B
CC or up-regulate NF-kappa-B-dependent survival signals. Moreover, mutant
CC animals are hyperphagic and exhibit higher food intake and reduced feed
CC efficiency versus wild type. Mice are considerably leaner and display
CC markedly decreased size of white fat depots. Triglyceride content in
CC the liver and skeletal muscle is also significantly low.
CC {ECO:0000269|PubMed:12118249, ECO:0000269|PubMed:17962198,
CC ECO:0000269|PubMed:8670417}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; X53532; CAA37611.1; -; mRNA.
DR EMBL; X59274; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC016522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC127083; AAI27084.1; -; mRNA.
DR CCDS; CCDS21815.1; -. [P68404-2]
DR CCDS; CCDS85402.1; -. [P68404-1]
DR PIR; S11213; S11213.
DR RefSeq; NP_001303601.1; NM_001316672.1. [P68404-1]
DR RefSeq; NP_032881.1; NM_008855.2. [P68404-2]
DR AlphaFoldDB; P68404; -.
DR SMR; P68404; -.
DR BioGRID; 202195; 36.
DR DIP; DIP-31583N; -.
DR IntAct; P68404; 16.
DR MINT; P68404; -.
DR STRING; 10090.ENSMUSP00000070019; -.
DR ChEMBL; CHEMBL3042; -.
DR iPTMnet; P68404; -.
DR PhosphoSitePlus; P68404; -.
DR SwissPalm; P68404; -.
DR EPD; P68404; -.
DR jPOST; P68404; -.
DR MaxQB; P68404; -.
DR PaxDb; P68404; -.
DR PeptideAtlas; P68404; -.
DR PRIDE; P68404; -.
DR ProteomicsDB; 264859; -. [P68404-1]
DR ProteomicsDB; 264860; -. [P68404-2]
DR Antibodypedia; 3547; 899 antibodies from 46 providers.
DR DNASU; 18751; -.
DR Ensembl; ENSMUST00000064921; ENSMUSP00000064812; ENSMUSG00000052889. [P68404-1]
DR Ensembl; ENSMUST00000064989; ENSMUSP00000070019; ENSMUSG00000052889. [P68404-2]
DR Ensembl; ENSMUST00000143692; ENSMUSP00000138788; ENSMUSG00000052889. [P68404-2]
DR GeneID; 18751; -.
DR KEGG; mmu:18751; -.
DR UCSC; uc009jot.1; mouse. [P68404-1]
DR UCSC; uc009jou.1; mouse. [P68404-2]
DR CTD; 5579; -.
DR MGI; MGI:97596; Prkcb.
DR VEuPathDB; HostDB:ENSMUSG00000052889; -.
DR eggNOG; KOG0696; Eukaryota.
DR GeneTree; ENSGT00940000155217; -.
DR HOGENOM; CLU_000288_54_2_1; -.
DR InParanoid; P68404; -.
DR OMA; YIAPEXA; -.
DR OrthoDB; 614710at2759; -.
DR TreeFam; TF351133; -.
DR BRENDA; 2.7.11.13; 3474.
DR Reactome; R-MMU-114516; Disinhibition of SNARE formation.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-76005; Response to elevated platelet cytosolic Ca2+.
DR BioGRID-ORCS; 18751; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Prkcb; mouse.
DR PRO; PR:P68404; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P68404; protein.
DR Bgee; ENSMUSG00000052889; Expressed in dorsal striatum and 244 other tissues.
DR Genevisible; P68404; MM.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0008091; C:spectrin; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005246; F:calcium channel regulator activity; IDA:MGI.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0035403; F:histone kinase activity (H3-T6 specific); ISS:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0004697; F:protein kinase C activity; IDA:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; IMP:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035408; P:histone H3-T6 phosphorylation; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; IMP:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:MGI.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR CDD; cd00029; C1; 2.
DR CDD; cd05616; STKc_cPKC_beta; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR034664; cPKC-beta.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014375; Protein_kinase_C_a/b/g.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000550; PKC_alpha; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Adaptive immunity; Alternative splicing; Apoptosis;
KW ATP-binding; Calcium; Chromatin regulator; Cytoplasm; Immunity; Kinase;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT CHAIN 2..671
FT /note="Protein kinase C beta type"
FT /id="PRO_0000055685"
FT DOMAIN 158..275
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 342..600
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 601..671
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 36..86
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 101..151
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 614..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 348..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 16
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT MOD_RES 17
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 250
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 314
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT MOD_RES 324
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT MOD_RES 500
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 635
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT MOD_RES 642
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05771"
FT MOD_RES 662
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000269|PubMed:12881490"
FT VAR_SEQ 622..671
FT /note="RDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV
FT -> CGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFVNSEFLKPEVKS (in
FT isoform Beta-II)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041812"
FT MOD_RES P68404-2:641
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES P68404-2:654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES P68404-2:660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES P68404-2:664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES P68404-2:673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 671 AA; 76751 MW; A1935030F758513C CRC64;
MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS
LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR EVLIVVVRDA
KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL
SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE
LRQKFERAKI GQGTKAPEEK TANTISKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE
RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM
EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI
KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP
FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF
RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF
SYTNPEFVIN V
