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P05771

- KPCB_HUMAN

UniProt

P05771 - KPCB_HUMAN

Protein

Protein kinase C beta type

Gene

PRKCB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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. 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 (ANDR)-dependent transcription, by being recruited to ANDR 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. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. 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.By similarity3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    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-500 (activation loop of the kinase domain), Thr-642 (turn motif) and Ser-661 (hydrophobic region), need to be phosphorylated for its full activation. Specifically inhibited by enzastaurin (LY317615).1 Publication

    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
    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 bindingi251 – 2511Calcium 3By similarity
    Metal bindingi252 – 2521Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi254 – 2541Calcium 1By similarity
    Metal bindingi254 – 2541Calcium 3By similarity
    Binding sitei371 – 3711ATPPROSITE-ProRule annotation
    Active sitei466 – 4661Proton 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 bindingi348 – 3569ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. calcium channel regulator activity Source: Ensembl
    4. chromatin binding Source: UniProtKB
    5. histone binding Source: UniProtKB
    6. histone kinase activity (H3-T6 specific) Source: UniProtKB
    7. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    8. protein binding Source: IntAct
    9. protein kinase C activity Source: ProtInc
    10. protein kinase C binding Source: UniProtKB
    11. protein serine/threonine kinase activity Source: Reactome
    12. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. B cell activation Source: UniProtKB
    3. B cell receptor signaling pathway Source: UniProtKB
    4. blood coagulation Source: Reactome
    5. calcium ion transport Source: Ensembl
    6. cellular calcium ion homeostasis Source: Ensembl
    7. cellular response to carbohydrate stimulus Source: Ensembl
    8. histone H3-T6 phosphorylation Source: UniProtKB
    9. intracellular signal transduction Source: InterPro
    10. lipoprotein transport Source: BHF-UCL
    11. negative regulation of glucose transport Source: UniProtKB
    12. negative regulation of insulin receptor signaling pathway Source: UniProtKB
    13. platelet activation Source: Reactome
    14. positive regulation of angiogenesis Source: UniProtKB
    15. positive regulation of B cell receptor signaling pathway Source: UniProtKB
    16. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    17. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    18. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    19. protein phosphorylation Source: ProtInc
    20. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    21. signal transduction Source: ProtInc
    22. synaptic transmission Source: Reactome
    23. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Adaptive immunity, Apoptosis, Immunity, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 2681.
    ReactomeiREACT_1178. Disinhibition of SNARE formation.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1280. Response to elevated platelet cytosolic Ca2+.
    REACT_172599. WNT5A-dependent internalization of FZD4.
    REACT_18422. Trafficking of GluR2-containing AMPA receptors.
    REACT_19333. G alpha (z) signalling events.
    REACT_200828. Depolymerisation of the Nuclear Lamina.
    SignaLinkiP05771.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C beta type (EC:2.7.11.13)
    Short name:
    PKC-B
    Short name:
    PKC-beta
    Gene namesi
    Name:PRKCB
    Synonyms:PKCB, PRKCB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9395. PRKCB.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus 1 Publication. Membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33761.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 671670Protein kinase C beta typePRO_0000055684Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei16 – 161Phosphoserine; by autocatalysisSequence Analysis
    Modified residuei17 – 171Phosphothreonine; by autocatalysisSequence Analysis
    Modified residuei250 – 2501Phosphothreonine; by autocatalysisBy similarity
    Modified residuei314 – 3141Phosphothreonine; by autocatalysisSequence Analysis
    Modified residuei324 – 3241Phosphothreonine; by autocatalysisSequence Analysis
    Modified residuei500 – 5001Phosphothreonine; by PDPK11 Publication
    Modified residuei504 – 5041Phosphothreonine1 Publication
    Modified residuei635 – 6351Phosphothreonine; by autocatalysis
    Modified residuei642 – 6421Phosphothreonine1 Publication
    Modified residuei661 – 6611Phosphoserine; by autocatalysis1 Publication
    Modified residuei662 – 6621Phosphotyrosine; by SYKBy similarity

    Post-translational modificationi

    Phosphorylation on Thr-500 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Autophosphorylation on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05771.
    PaxDbiP05771.
    PRIDEiP05771.

    PTM databases

    PhosphoSiteiP05771.

    Miscellaneous databases

    PMAP-CutDBP05771.

    Expressioni

    Gene expression databases

    ArrayExpressiP05771.
    BgeeiP05771.
    GenevestigatoriP05771.

    Organism-specific databases

    HPAiCAB003843.

    Interactioni

    Subunit structurei

    Interacts with PDK1 By similarity. Interacts in vitro with PRKCBP1. Interacts with PHLPP1 and PHLPP2; both proteins mediate its dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and ANDR.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PHLPP1O603465EBI-5774511,EBI-2511516

    Protein-protein interaction databases

    BioGridi111565. 57 interactions.
    DIPiDIP-34187N.
    IntActiP05771. 18 interactions.
    MINTiMINT-240997.

    Structurei

    Secondary structure

    1
    671
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi342 – 35110
    Beta strandi354 – 3618
    Beta strandi364 – 37411
    Helixi375 – 3806
    Helixi384 – 39411
    Beta strandi406 – 4116
    Beta strandi413 – 4219
    Helixi428 – 4358
    Helixi440 – 45920
    Helixi469 – 4713
    Beta strandi472 – 4743
    Beta strandi480 – 4823
    Helixi505 – 5073
    Helixi510 – 5134
    Helixi521 – 53616
    Helixi546 – 55510
    Helixi566 – 57510
    Helixi590 – 5956
    Helixi598 – 6003
    Helixi605 – 6095
    Helixi629 – 6368
    Turni654 – 6574

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I0EX-ray2.60A/B321-671[»]
    ProteinModelPortaliP05771.
    SMRiP05771. Positions 37-668.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05771.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini173 – 26088C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini342 – 600259Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini601 – 67171AGC-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.
    HOVERGENiHBG108317.
    KOiK02677.
    OMAiQAHIDRE.
    OrthoDBiEOG77M8QM.
    PhylomeDBiP05771.
    TreeFamiTF351133.

    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.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014375. Protein_kinase_C_a/b/g.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Beta-I (identifier: P05771-1) [UniParc]FASTAAdd to Basket

    Also known as: PRKCB1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC    50
    SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS 100
    KHKFKIHTYS SPTFCDHCGS LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL 150
    CGTDHTERRG RIYIQAHIDR DVLIVLVRDA KNLVPMDPNG LSDPYVKLKL 200
    IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL SVEIWDWDLT 250
    SRNDFMGSLS FGISELQKAS VDGWFKLLSQ EEGEYFNVPV PPEGSEANEE 300
    LRQKFERAKI SQGTKVPEEK TTNTVSKFDN NGNRDRMKLT DFNFLMVLGK 350
    GSFGKVMLSE RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP 400
    PFLTQLHSCF QTMDRLYFVM EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI 450
    AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI KIADFGMCKE NIWDGVTTKT 500
    FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP FEGEDEDELF 550
    QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF 600
    RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM 650
    NLDQNEFAGF SYTNPEFVIN V 671
    Length:671
    Mass (Da):76,869
    Last modified:January 23, 2007 - v4
    Checksum:i3937E7B667108C68
    GO
    Isoform Beta-II (identifier: P05771-2) [UniParc]FASTAAdd to Basket

    Also known as: PRKCB2

    The sequence of this isoform differs from the canonical sequence as follows:
         622-671: RDKRDTSNFD...YTNPEFVINV → CGRNAENFDR...SEFLKPEVKS

    Note: Contains a phosphoserine at position 660. Contains a phosphothreonine at position 641.

    Show »
    Length:673
    Mass (Da):77,012
    Checksum:i03D42B0E4164B48F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti69 – 691V → G in CAA44393. (PubMed:7880442)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441V → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042304
    Natural varianti496 – 4961V → M in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_042305
    Natural varianti588 – 5881P → H.1 Publication
    Corresponds to variant rs35631544 [ dbSNP | Ensembl ].
    VAR_042306

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei622 – 67150RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II. 2 PublicationsVSP_004738Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13975 mRNA. Translation: AAA60095.1.
    X06318 mRNA. Translation: CAA29634.1.
    X07109 mRNA. Translation: CAA30130.1.
    FJ907246 Genomic DNA. Translation: ACS14045.1.
    AC130454 Genomic DNA. No translation available.
    AC002299 Genomic DNA. Translation: AAB97933.1.
    AC002299 Genomic DNA. Translation: AAB97934.1.
    CH471145 Genomic DNA. Translation: EAW55797.1.
    CH471145 Genomic DNA. Translation: EAW55798.1.
    BC036472 mRNA. Translation: AAH36472.1.
    X62532 Genomic DNA. Translation: CAA44393.1.
    S47311 Genomic DNA. Translation: AAD13852.1.
    D10022 Genomic DNA. Translation: BAA00912.1.
    AJ002799, AJ002800 Genomic DNA. Translation: CAA05725.1.
    M18254 Genomic DNA. Translation: AAA60096.1.
    M18255 Genomic DNA. Translation: AAA60097.1.
    X05972 Genomic DNA. Translation: CAA29396.1.
    X05971 Genomic DNA. Translation: CAA29395.1.
    CCDSiCCDS10618.1. [P05771-1]
    CCDS10619.1. [P05771-2]
    PIRiB24664. KIHUC2.
    S00159. KIHUC1.
    RefSeqiNP_002729.2. NM_002738.6. [P05771-2]
    NP_997700.1. NM_212535.2. [P05771-1]
    UniGeneiHs.460355.

    Genome annotation databases

    EnsembliENST00000303531; ENSP00000305355; ENSG00000166501. [P05771-2]
    ENST00000321728; ENSP00000318315; ENSG00000166501. [P05771-1]
    ENST00000498058; ENSP00000454428; ENSG00000166501.
    GeneIDi5579.
    KEGGihsa:5579.
    UCSCiuc002dmd.3. human. [P05771-1]
    uc002dme.3. human. [P05771-2]

    Polymorphism databases

    DMDMi20141488.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13975 mRNA. Translation: AAA60095.1 .
    X06318 mRNA. Translation: CAA29634.1 .
    X07109 mRNA. Translation: CAA30130.1 .
    FJ907246 Genomic DNA. Translation: ACS14045.1 .
    AC130454 Genomic DNA. No translation available.
    AC002299 Genomic DNA. Translation: AAB97933.1 .
    AC002299 Genomic DNA. Translation: AAB97934.1 .
    CH471145 Genomic DNA. Translation: EAW55797.1 .
    CH471145 Genomic DNA. Translation: EAW55798.1 .
    BC036472 mRNA. Translation: AAH36472.1 .
    X62532 Genomic DNA. Translation: CAA44393.1 .
    S47311 Genomic DNA. Translation: AAD13852.1 .
    D10022 Genomic DNA. Translation: BAA00912.1 .
    AJ002799 , AJ002800 Genomic DNA. Translation: CAA05725.1 .
    M18254 Genomic DNA. Translation: AAA60096.1 .
    M18255 Genomic DNA. Translation: AAA60097.1 .
    X05972 Genomic DNA. Translation: CAA29396.1 .
    X05971 Genomic DNA. Translation: CAA29395.1 .
    CCDSi CCDS10618.1. [P05771-1 ]
    CCDS10619.1. [P05771-2 ]
    PIRi B24664. KIHUC2.
    S00159. KIHUC1.
    RefSeqi NP_002729.2. NM_002738.6. [P05771-2 ]
    NP_997700.1. NM_212535.2. [P05771-1 ]
    UniGenei Hs.460355.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I0E X-ray 2.60 A/B 321-671 [» ]
    ProteinModelPortali P05771.
    SMRi P05771. Positions 37-668.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111565. 57 interactions.
    DIPi DIP-34187N.
    IntActi P05771. 18 interactions.
    MINTi MINT-240997.

    Chemistry

    BindingDBi P05771.
    ChEMBLi CHEMBL3045.
    DrugBanki DB00163. Vitamin E.
    GuidetoPHARMACOLOGYi 1483.

    PTM databases

    PhosphoSitei P05771.

    Polymorphism databases

    DMDMi 20141488.

    Proteomic databases

    MaxQBi P05771.
    PaxDbi P05771.
    PRIDEi P05771.

    Protocols and materials databases

    DNASUi 5579.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303531 ; ENSP00000305355 ; ENSG00000166501 . [P05771-2 ]
    ENST00000321728 ; ENSP00000318315 ; ENSG00000166501 . [P05771-1 ]
    ENST00000498058 ; ENSP00000454428 ; ENSG00000166501 .
    GeneIDi 5579.
    KEGGi hsa:5579.
    UCSCi uc002dmd.3. human. [P05771-1 ]
    uc002dme.3. human. [P05771-2 ]

    Organism-specific databases

    CTDi 5579.
    GeneCardsi GC16P023847.
    HGNCi HGNC:9395. PRKCB.
    HPAi CAB003843.
    MIMi 176970. gene.
    neXtProti NX_P05771.
    PharmGKBi PA33761.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG108317.
    KOi K02677.
    OMAi QAHIDRE.
    OrthoDBi EOG77M8QM.
    PhylomeDBi P05771.
    TreeFami TF351133.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 2681.
    Reactomei REACT_1178. Disinhibition of SNARE formation.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1280. Response to elevated platelet cytosolic Ca2+.
    REACT_172599. WNT5A-dependent internalization of FZD4.
    REACT_18422. Trafficking of GluR2-containing AMPA receptors.
    REACT_19333. G alpha (z) signalling events.
    REACT_200828. Depolymerisation of the Nuclear Lamina.
    SignaLinki P05771.

    Miscellaneous databases

    ChiTaRSi PRKCB. human.
    EvolutionaryTracei P05771.
    GeneWikii PRKCB1.
    GenomeRNAii 5579.
    NextBioi 21632.
    PMAP-CutDB P05771.
    PROi P05771.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05771.
    Bgeei P05771.
    Genevestigatori P05771.

    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.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014375. Protein_kinase_C_a/b/g.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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. "Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways."
      Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A.
      Science 233:859-866(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II).
    2. "Primary structures of human protein kinase C beta I and beta II differ only in their C-terminal sequences."
      Kubo K., Ohno S., Suzuki K.
      FEBS Lett. 223:138-142(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II).
    3. NIEHS SNPs program
      Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Hippocampus.
    7. "Autoregulation of cloned human protein kinase C beta and gamma gene promoters in U937 cells."
      Mahajna J., King P., Parker P., Haley J.
      DNA Cell Biol. 14:213-222(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
    8. "Positive and negative regulation of the transcription of the human protein kinase C beta gene."
      Niino Y.S., Ohno S., Suzuki K.
      J. Biol. Chem. 267:6158-6163(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
    9. "Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters."
      Obeid L.M., Blobe G.C., Karolak L.A., Hannun Y.A.
      J. Biol. Chem. 267:20804-20810(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
    10. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-19, ACETYLATION AT ALA-2.
      Tissue: Platelet.
    11. "The genomic structure of the human protein kinase C beta gene (PRKCB)."
      Greenham J.A., Adams M.D., Doggett N.A., Mole S.E.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-176.
    12. "Alternative splicing increases the diversity of the human protein kinase C family."
      Coussens L., Rhee L., Parker P.J., Ullrich A.
      DNA 6:389-394(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-671.
      Tissue: Fetal brain.
    13. "Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta-I/beta-II."
      Kubo K., Ohno S., Suzuki K.
      Nucleic Acids Res. 15:7179-7180(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-671.
    14. "PKCbeta modulates antigen receptor signaling via regulation of Btk membrane localization."
      Kang S.W., Wahl M.I., Chu J., Kitaura J., Kawakami Y., Kato R.M., Tabuchi R., Tarakhovsky A., Kawakami T., Turck C.W., Witte O.N., Rawlings D.J.
      EMBO J. 20:5692-5702(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BTK.
    15. "The protein kinase Cbeta-selective inhibitor, enzastaurin (LY317615.HCl), suppresses signaling through the AKT pathway, induces apoptosis, and suppresses growth of human colon cancer and glioblastoma xenografts."
      Graff J.R., McNulty A.M., Hanna K.R., Konicek B.W., Lynch R.L., Bailey S.N., Banks C., Capen A., Goode R., Lewis J.E., Sams L., Huss K.L., Campbell R.M., Iversen P.W., Neubauer B.L., Brown T.J., Musib L., Geeganage S., Thornton D.
      Cancer Res. 65:7462-7469(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    16. "The phosphatase PHLPP controls the cellular levels of protein kinase C."
      Gao T., Brognard J., Newton A.C.
      J. Biol. Chem. 283:6300-6311(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHLPP1 AND PHLPP2.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    18. "Phosphorylation of activation transcription factor-2 at serine 121 by protein kinase c controls c-Jun-mediated activation of transcription."
      Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.
      J. Biol. Chem. 284:8567-8581(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641 AND SER-660 (ISOFORM BETA-II), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: FUNCTION IN HISTONE H3 PHOSPHORYLATION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH KDM1A; PKN1 AND ANDR.
    21. "Protein kinase C beta (PKC beta): normal functions and diseases."
      Kawakami T., Kawakami Y., Kitaura J.
      J. Biochem. 132:677-682(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    22. "Endothelial dysfunction in diabetes mellitus: molecular mechanisms and clinical implications."
      Tabit C.E., Chung W.B., Hamburg N.M., Vita J.A.
      Rev. Endocr. Metab. Disord. 11:61-74(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Structure of the catalytic domain of human protein kinase C beta II complexed with a bisindolylmaleimide inhibitor."
      Grodsky N., Li Y., Bouzida D., Love R., Jensen J., Nodes B., Nonomiya J., Grant S.
      Biochemistry 45:13970-13981(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 321-660 IN COMPLEX WITH INHIBITOR, PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
    25. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-144; MET-496 AND HIS-588.

    Entry informationi

    Entry nameiKPCB_HUMAN
    AccessioniPrimary (citable) accession number: P05771
    Secondary accession number(s): C5IFJ8
    , D3DWF5, O43744, P05127, Q15138, Q93060, Q9UE49, Q9UE50, Q9UEH8, Q9UJ30, Q9UJ33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 190 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3