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P68404

- KPCB_MOUSE

UniProt

P68404 - KPCB_MOUSE

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Protein

Protein kinase C beta type

Gene

Prkcb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Ca2+By similarityNote: Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain.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) (By similarity).By similarity

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: MGI
  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 kinase C activity Source: MGI
  9. 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. calcium ion transport Source: MGI
  5. cellular calcium ion homeostasis Source: MGI
  6. cellular response to carbohydrate stimulus Source: MGI
  7. histone H3-T6 phosphorylation Source: UniProtKB
  8. intracellular signal transduction Source: InterPro
  9. negative regulation of glucose transport Source: UniProtKB
  10. negative regulation of insulin receptor signaling pathway Source: UniProtKB
  11. positive regulation of angiogenesis Source: UniProtKB
  12. positive regulation of B cell receptor signaling pathway Source: UniProtKB
  13. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  14. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  15. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  16. protein phosphorylation Source: MGI
  17. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  18. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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

ReactomeiREACT_199121. Activation of NF-kappaB in B cells.
REACT_206166. Response to elevated platelet cytosolic Ca2+.
REACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_215302. Disinhibition of SNARE formation.
REACT_222404. WNT5A-dependent internalization of FZD4.
REACT_245086. VEGFR2 mediated cell proliferation.
REACT_253367. Trafficking of GluR2-containing AMPA receptors.
REACT_258013. G alpha (z) signalling events.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:97596. Prkcb.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice develop an immunodeficiency characterized by impaired humoral immune responses and reduced cellular responses of B-cells similar to X-linked immunodeficiency (Xid). Mice are unable to activate NF-kappa-B and promote cell survival in B-cells upon BCR signaling, or even in mast cells. B-cells fail to recruit the I-kappa-B kinase (IKK) complex into lipid rafts, activate IKK, degrade I-kappa-B or up-regulate NF-kappa-B-dependent survival signals. Moreover, mutant animals are hyperphagic and exhibit higher food intake and reduced feed efficiency versus wild type. Mice are considerably leaner and display markedly decreased size of white fat depots. Triglyceride content in the liver and skeletal muscle is also significantly low.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 671670Protein kinase C beta typePRO_0000055685Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei16 – 161Phosphoserine; by autocatalysisBy similarity
Modified residuei17 – 171Phosphothreonine; by autocatalysisBy similarity
Modified residuei250 – 2501Phosphothreonine; by autocatalysisBy similarity
Modified residuei314 – 3141Phosphothreonine; by autocatalysisBy similarity
Modified residuei324 – 3241Phosphothreonine; by autocatalysisBy similarity
Modified residuei500 – 5001Phosphothreonine; by PDPK1By similarity
Modified residuei504 – 5041PhosphothreonineBy similarity
Modified residuei635 – 6351Phosphothreonine; by autocatalysisBy similarity
Modified residuei642 – 6421Phosphothreonine; by autocatalysisBy similarity
Modified residuei661 – 6611PhosphoserineBy similarity
Modified residuei662 – 6621Phosphotyrosine; by SYK1 Publication

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 (By similarity). Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade.By similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP68404.
PaxDbiP68404.
PRIDEiP68404.

PTM databases

PhosphoSiteiP68404.

Expressioni

Gene expression databases

BgeeiP68404.
GenevestigatoriP68404.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
BMPR2Q138734EBI-397048,EBI-527196From a different organism.
EIF6P565372EBI-397048,EBI-372243From a different organism.

Protein-protein interaction databases

BioGridi202195. 8 interactions.
DIPiDIP-31583N.
IntActiP68404. 6 interactions.
MINTiMINT-98059.

Structurei

3D structure databases

ProteinModelPortaliP68404.
SMRiP68404. Positions 37-668.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00770000120449.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP68404.
KOiK02677.
OMAiQAHIDRE.
OrthoDBiEOG77M8QM.
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.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR002290. Ser/Thr_dual-sp_kinase.
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: P68404-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC
60 70 80 90 100
SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS
110 120 130 140 150
KHKFKIHTYS SPTFCDHCGS LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL
160 170 180 190 200
CGTDHTERRG RIYIQAHIDR EVLIVVVRDA KNLVPMDPNG LSDPYVKLKL
210 220 230 240 250
IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL SVEIWDWDLT
260 270 280 290 300
SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE
310 320 330 340 350
LRQKFERAKI GQGTKAPEEK TANTISKFDN NGNRDRMKLT DFNFLMVLGK
360 370 380 390 400
GSFGKVMLSE RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP
410 420 430 440 450
PFLTQLHSCF QTMDRLYFVM EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI
460 470 480 490 500
AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI KIADFGMCKE NIWDGVTTKT
510 520 530 540 550
FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP FEGEDEDELF
560 570 580 590 600
QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF
610 620 630 640 650
RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM
660 670
NLDQNEFAGF SYTNPEFVIN V
Length:671
Mass (Da):76,751
Last modified:September 21, 2011 - v4
Checksum:iA1935030F758513C
GO
Isoform Beta-II (identifier: P68404-2) [UniParc]FASTAAdd to Basket

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

Note: Contains a phosphothreonine at position 641.

Show »
Length:673
Mass (Da):76,894
Checksum:iA65573AAF6E224C7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei622 – 67150RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II. 1 PublicationVSP_041812Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53532 mRNA. Translation: CAA37611.1.
X59274 mRNA. No translation available.
AC016522 Genomic DNA. No translation available.
AC122232 Genomic DNA. No translation available.
AC123837 Genomic DNA. No translation available.
AC151986 Genomic DNA. No translation available.
BC127083 mRNA. Translation: AAI27084.1.
CCDSiCCDS21815.1. [P68404-2]
PIRiS11213.
RefSeqiNP_032881.1. NM_008855.2. [P68404-2]
XP_006507505.1. XM_006507442.1. [P68404-1]
UniGeneiMm.207496.
Mm.446371.

Genome annotation databases

EnsembliENSMUST00000064921; ENSMUSP00000064812; ENSMUSG00000052889. [P68404-1]
ENSMUST00000064989; ENSMUSP00000070019; ENSMUSG00000052889. [P68404-2]
ENSMUST00000143692; ENSMUSP00000138788; ENSMUSG00000052889. [P68404-2]
GeneIDi18751.
KEGGimmu:18751.
UCSCiuc009jot.1. mouse. [P68404-1]
uc009jou.1. mouse. [P68404-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53532 mRNA. Translation: CAA37611.1 .
X59274 mRNA. No translation available.
AC016522 Genomic DNA. No translation available.
AC122232 Genomic DNA. No translation available.
AC123837 Genomic DNA. No translation available.
AC151986 Genomic DNA. No translation available.
BC127083 mRNA. Translation: AAI27084.1 .
CCDSi CCDS21815.1. [P68404-2 ]
PIRi S11213.
RefSeqi NP_032881.1. NM_008855.2. [P68404-2 ]
XP_006507505.1. XM_006507442.1. [P68404-1 ]
UniGenei Mm.207496.
Mm.446371.

3D structure databases

ProteinModelPortali P68404.
SMRi P68404. Positions 37-668.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202195. 8 interactions.
DIPi DIP-31583N.
IntActi P68404. 6 interactions.
MINTi MINT-98059.

Chemistry

BindingDBi P68404.

PTM databases

PhosphoSitei P68404.

Proteomic databases

MaxQBi P68404.
PaxDbi P68404.
PRIDEi P68404.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000064921 ; ENSMUSP00000064812 ; ENSMUSG00000052889 . [P68404-1 ]
ENSMUST00000064989 ; ENSMUSP00000070019 ; ENSMUSG00000052889 . [P68404-2 ]
ENSMUST00000143692 ; ENSMUSP00000138788 ; ENSMUSG00000052889 . [P68404-2 ]
GeneIDi 18751.
KEGGi mmu:18751.
UCSCi uc009jot.1. mouse. [P68404-1 ]
uc009jou.1. mouse. [P68404-2 ]

Organism-specific databases

CTDi 5579.
MGIi MGI:97596. Prkcb.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120449.
HOGENOMi HOG000233022.
HOVERGENi HBG108317.
InParanoidi P68404.
KOi K02677.
OMAi QAHIDRE.
OrthoDBi EOG77M8QM.
TreeFami TF351133.

Enzyme and pathway databases

Reactomei REACT_199121. Activation of NF-kappaB in B cells.
REACT_206166. Response to elevated platelet cytosolic Ca2+.
REACT_208718. Depolymerisation of the Nuclear Lamina.
REACT_215302. Disinhibition of SNARE formation.
REACT_222404. WNT5A-dependent internalization of FZD4.
REACT_245086. VEGFR2 mediated cell proliferation.
REACT_253367. Trafficking of GluR2-containing AMPA receptors.
REACT_258013. G alpha (z) signalling events.

Miscellaneous databases

ChiTaRSi Prkcb. mouse.
NextBioi 294921.
PROi P68404.
SOURCEi Search...

Gene expression databases

Bgeei P68404.
Genevestigatori P68404.

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.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR002290. Ser/Thr_dual-sp_kinase.
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

« Hide 'large scale' publications
  1. "Isolation of cloned mouse protein kinase C beta-II cDNA and its sequence."
    Tang Y.-M., Ashendel C.L.
    Nucleic Acids Res. 18:5310-5310(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-I).
    Strain: ICR X Swiss Webster.
    Tissue: Brain.
  2. "Nucleotide sequence of cDNA for mouse brain protein kinase C beta-I subspecies."
    Powell C.T.
    Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] (ISOFORMS BETA-I).
  5. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Effects of knockout of the protein kinase C beta gene on glucose transport and glucose homeostasis."
    Standaert M.L., Bandyopadhyay G., Galloway L., Soto J., Ono Y., Kikkawa U., Farese R.V., Leitges M.
    Endocrinology 140:4470-4477(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INSULIN SIGNALING.
  7. "Protein kinase C beta controls nuclear factor kappaB activation in B cells through selective regulation of the IkappaB kinase alpha."
    Saijo K., Mecklenbrauker I., Santana A., Leitger M., Schmedt C., Tarakhovsky A.
    J. Exp. Med. 195:1647-1652(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "PKC-beta controls I kappa B kinase lipid raft recruitment and activation in response to BCR signaling."
    Su T.T., Guo B., Kawakami Y., Sommer K., Chae K., Humphries L.A., Kato R.M., Kang S., Patrone L., Wall R., Teitell M., Leitges M., Kawakami T., Rawlings D.J.
    Nat. Immunol. 3:780-786(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "Characterization of protein kinase C beta isoform's action on retinoblastoma protein phosphorylation, vascular endothelial growth factor-induced endothelial cell proliferation, and retinal neovascularization."
    Suzuma K., Takahara N., Suzuma I., Isshiki K., Ueki K., Leitges M., Aiello L.P., King G.L.
    Proc. Natl. Acad. Sci. U.S.A. 99:721-726(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOTHELIAL CELLS PROLIFERATION.
  10. Cited for: PHOSPHORYLATION AT TYR-662.
  11. Cited for: FUNCTION, INTERACTION WITH CARD11.
  12. "PKC beta regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1."
    Shinohara H., Yasuda T., Aiba Y., Sanjo H., Hamadate M., Watarai H., Sakurai H., Kurosaki T.
    J. Exp. Med. 202:1423-1431(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION.
  13. "Activation of vascular protein kinase C-beta inhibits Akt-dependent endothelial nitric oxide synthase function in obesity-associated insulin resistance."
    Naruse K., Rask-Madsen C., Takahara N., Ha S.W., Suzuma K., Way K.J., Jacobs J.R., Clermont A.C., Ueki K., Ohshiro Y., Zhang J., Goldfine A.B., King G.L.
    Diabetes 55:691-698(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOTHELIAL CELLS.
  14. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641 (ISOFORM BETA-II), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  15. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  16. "Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc."
    Pinton P., Rimessi A., Marchi S., Orsini F., Migliaccio E., Giorgio M., Contursi C., Minucci S., Mantovani F., Wieckowski M.R., Del Sal G., Pelicci P.G., Rizzuto R.
    Science 315:659-663(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Protein kinase C deficiency increases fatty acid oxidation and reduces fat storage."
    Bansode R.R., Huang W., Roy S.K., Mehta M., Mehta K.D.
    J. Biol. Chem. 283:231-236(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiKPCB_MOUSE
AccessioniPrimary (citable) accession number: P68404
Secondary accession number(s): A0JNZ5
, F2Z441, P04410, P04411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: September 21, 2011
Last modified: November 26, 2014
This is version 119 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3