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 04-NOV-2026, entry version 205. DE RecName: Full=Protein kinase C beta type; DE Short=PKC-B; DE Short=PKC-beta; DE EC=2.7.11.13 {ECO:0000250|UniProtKB:P05771}; 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). RN [19] RP PHOSPHORYLATION AT THR-634 (ISOFORM BETA-II). RX PubMed=33850054; DOI=10.1126/scisignal.abe4509; RA Baffi T.R., Lorden G., Wozniak J.M., Feichtner A., Yeung W., Kornev A.P., RA King C.C., Del Rio J.C., Limaye A.J., Bogomolovas J., Gould C.M., Chen J., RA Kennedy E.J., Kannan N., Gonzalez D.J., Stefan E., Taylor S.S., RA Newton A.C.; RT "mTORC2 controls the activity of PKC and Akt by phosphorylating a conserved RT TOR interaction motif."; RL Sci. Signal. 14:0-0(2021). 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). Phosphorylates KLHL3 in response to angiotensin II CC signaling, decreasing the interaction between KLHL3 and WNK4 (By CC similarity). Phosphorylates and activates LRRK1, which phosphorylates CC RAB proteins involved in intracellular trafficking (By similarity). CC Acts as a regulator of dopamine signaling by mediating constitutive CC phosphorylation of dopamine receptors DRD1 and DRD2, inhibiting G CC protein-coupled receptor signaling (By similarity). CC {ECO:0000250|UniProtKB:P05771, ECO:0000269|PubMed:10499500, CC ECO:0000269|PubMed:11805327, ECO:0000269|PubMed:12070292, CC ECO:0000269|PubMed:12118249, ECO:0000269|PubMed:16301747, CC ECO:0000269|PubMed:16356855, ECO:0000269|PubMed:16505232, CC ECO:0000269|PubMed:17272725, ECO:0000269|PubMed:8670417}. CC -!- FUNCTION: [Isoform Beta-II]: Acts as an activator of ferroptosis by CC mediating phosphorylation and activation of ACSL4. Also stimulates CC ferroptosis propagation by catalyzing phosphorylation of FOXK1. CC {ECO:0000250|UniProtKB:P05771}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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 Evidence={ECO:0000250|UniProtKB:P05771}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; CC Evidence={ECO:0000250|UniProtKB:P05771}; CC -!- CATALYTIC ACTIVITY: [Isoform Beta-II]: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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 Evidence={ECO:0000250|UniProtKB:P05771}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000250|UniProtKB:P05771}; CC -!- CATALYTIC ACTIVITY: [Isoform Beta-II]: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; CC Evidence={ECO:0000250|UniProtKB:P05771}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000250|UniProtKB:P05771}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC 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 PDPK1/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 -!- PTM: [Isoform Beta-II]: In response to growth factors, phosphorylated CC at Thr-634 by the mTORC2 complex, promoting autophosphorylation and CC activation. {ECO:0000269|PubMed:33850054}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 40. DR CORUM; P68404; -. DR DIP; DIP-31583N; -. DR FunCoup; P68404; 1872. DR IntAct; P68404; 16. DR STRING; 10090.ENSMUSP00000070019; -. DR ChEMBL; CHEMBL3042; -. DR GlyCosmos; P68404; 1 site, 1 glycan. DR GlyGen; P68404; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P68404; -. DR PhosphoSitePlus; P68404; -. DR SwissPalm; P68404; -. DR jPOST; P68404; -. DR PaxDb; 10090-ENSMUSP00000070019; -. DR PeptideAtlas; P68404; -. DR ProteomicsDB; 264859; -. [P68404-1] DR ProteomicsDB; 264860; -. [P68404-2] DR Pumba; P68404; -. DR Antibodypedia; 3547; 1003 antibodies from 49 providers. DR DNASU; 18751; -. DR Ensembl; ENSMPUT00000012299; ENSMPUP00000012100; ENSMPUG00000012196. DR Ensembl; ENSMUST00000064921.5; ENSMUSP00000064812.5; ENSMUSG00000052889.12. [P68404-1] DR Ensembl; ENSMUST00000064989.12; ENSMUSP00000070019.6; ENSMUSG00000052889.12. [P68404-2] DR Ensembl; ENSMUST00000143692.8; ENSMUSP00000138788.2; ENSMUSG00000052889.12. [P68404-2] DR GeneID; 18751; -. DR KEGG; mmu:18751; -. DR UCSC; uc009jot.1; mouse. [P68404-1] DR UCSC; uc009jou.1; mouse. [P68404-2] DR AGR; MGI:97596; -. 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 OrthoDB; 3664at9989; -. 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; Depolymerization 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 82 CRISPR screens. DR CD-CODE; 453FB656; Mast cell extracellular granules (MCEGs). DR PRO; PR:P68404; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P68404; protein. DR Bgee; ENSMUSG00000052889; Expressed in dorsal striatum and 246 other cell types or tissues. DR GO; GO:0031526; C:brush border membrane; ISO:GO_Central. DR GO; GO:0044305; C:calyx of Held; IDA:SynGO. DR GO; GO:0005813; C:centrosome; ISO:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:GO_Central. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA: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:InterPro. DR GO; GO:0005246; F:calcium channel regulator activity; IDA:MGI. DR GO; GO:0004698; F:calcium,diacylglycerol-dependent serine/threonine kinase activity; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IDA:MGI. DR GO; GO:0042393; F:histone binding; ISS:UniProtKB. DR GO; GO:0035403; F:histone H3T6 kinase activity; ISS:UniProtKB. DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB. DR GO; GO:0005080; F:protein kinase C binding; ISO:GO_Central. DR GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI. DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. 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:0071322; P:cellular response to carbohydrate stimulus; IDA:MGI. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:MGI. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0010829; P:negative regulation of D-glucose transmembrane transport; IMP:UniProtKB. DR GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0007207; P:phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway; IDA:MGI. DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB. DR GO; GO:0160020; P:positive regulation of ferroptosis; ISS:UniProtKB. DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0070528; P:protein kinase C signaling; ISS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI. DR GO; GO:0010827; P:regulation of D-glucose transmembrane transport; ISS:UniProtKB. DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:GO_Central. DR GO; GO:0040008; P:regulation of growth; ISO:GO_Central. 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:1990776; P:response to angiotensin; ISO:GO_Central. DR GO; GO:0001666; P:response to hypoxia; IDA:MGI. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:GO_Central. DR CDD; cd20833; C1_cPKC_rpt1; 1. DR CDD; cd20836; C1_cPKC_rpt2; 1. DR CDD; cd04026; C2_PKC_alpha_gamma; 1. DR CDD; cd05616; STKc_cPKC_beta; 1. DR FunFam; 2.60.40.150:FF:000012; Kinase C alpha type; 1. DR FunFam; 1.10.510.10:FF:000023; Protein kinase C; 1. DR FunFam; 3.30.60.20:FF:000006; Protein kinase C; 1. DR FunFam; 3.30.60.20:FF:000031; Protein kinase C alpha; 1. DR FunFam; 3.30.200.20:FF:000601; Protein kinase C epsilon; 1. DR Gene3D; 3.30.60.20; -; 2. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; PKC_DAG/PE. 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 PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. 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; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. 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 623..635 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 P68404-2:634 FT /note="Phosphothreonine; by MTOR" FT /evidence="ECO:0000269|PubMed:33850054" 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 //