Protein kinase C beta type (PKC-B) (PKC-beta) (EC 2.7.11.13)
1_MADPA 6_ AGPPP 11_ SEGEE 16_ STVRF 21_ ARKGA 26_ LRQKN 31_ VHEVK 36_ NHKFT 41_ ARFFK 46_ QPTFC 51_ SHCTD 56_ FIWGF 61_ GKQGF 66_ QCQVC 71_ CFVVH 76_ KRCHE 81_ FVTFS 86_ CPGAD 91_ KGPAS 96_ DDPRS 101_ KHKFK 106_ IHTYS 111_ SPTFC 116_ DHCGS 121_ LLYGL 126_ IHQGM 131_ KCDTC 136_ MMNVH 141_ KRCVM 146_ NVPSL 151_ CGTDH 156_ TERRG 161_ RIYIQ 166_ AHIDR 171_ DVLIV 176_ LVRDA 181_ KNLVP 186_ MDPNG 191_ LSDPY 196_ VKLKL 201_ IPDPK 206_ SESKQ 211_ KTKTI 216_ KCSLN 221_ PEWNE 226_ TFRFQ 231_ LKESD 236_ KDRRL 241_ SVEIW 246_ DWDLT 251_ SRNDF 256_ MGSLS 261_ FGISE 266_ LQKAS 271_ VDGWF 276_ KLLSQ 281_ EEGEY 286_ FNVPV 291_ PPEGS 296_ EANEE 301_ LRQKF 306_ ERAKI 311_ SQGTK 316_ VPEEK 321_ TTNTV 326_ SKFDN 331_ NGNRD 336_ RMKLT 341_ DFNFL 346_ MVLGK 351_ GSFGK 356_ VMLSE 361_ RKGTD 366_ ELYAV 371_ KILKK 376_ DVVIQ 381_ DDDVE 386_ CTMVE 391_ KRVLA 396_ LPGKP 401_ PFLTQ 406_ LHSCF 411_ QTMDR 416_ LYFVM 421_ EYVNG 426_ GDLMY 431_ HIQQV 436_ GRFKE 441_ PHAVF 446_ YAAEI 451_ AIGLF 456_ FLQSK 461_ GIIYR 466_ DLKLD 471_ NVMLD 476_ SEGHI 481_ KIADF 486_ GMCKE 491_ NIWDG 496_ VTTKT 501_ FCGTP 506_ DYIAP 511_ EIIAY 516_ QPYGK 521_ SVDWW 526_ AFGVL 531_ LYEML 536_ AGQAP 541_ FEGED 546_ EDELF 551_ QSIME 556_ HNVAY 561_ PKSMS 566_ KEAVA 571_ ICKGL 576_ MTKHP 581_ GKRLG 586_ CGPEG 591_ ERDIK 596_ EHAFF 601_ RYIDW 606_ EKLER 611_ KEIQP 616_ PYKPK 621_ ARDKR 626_ DTSNF 631_ DKEFT 636_ RQPVE 641_ LTPTD 646_ KLFIM 651_ NLDQN 656_ EFAGF 661_ SYTNP 666_EFVIN
1: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity (PubMed:11598012). Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A (PubMed:20228790). In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1 (PubMed:25982116). Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (PubMed:19176525). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231)