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P05771 (KPCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 184. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C beta type

Short name=PKC-B
Short name=PKC-beta
EC=2.7.11.13
Gene names
Name:PRKCB
Synonyms:PKCB, PRKCB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length671 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 p66Shcof 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. Ref.14 Ref.18 Ref.20

Catalytic activity

ATP + a protein = ADP + a phosphoprotein. Ref.20

Cofactor

Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity.

Enzyme regulation

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). Ref.15

Subunit structure

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. Ref.16 Ref.20

Subcellular location

Cytoplasm By similarity. Nucleus. Membrane; Peripheral membrane protein By similarity Ref.20.

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Apoptosis
Immunity
Transcription
Transcription regulation
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionChromatin regulator
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

B cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion transport

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to carbohydrate stimulus

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipoprotein transport

Traceable author statement PubMed 18981301. Source: BHF-UCL

negative regulation of glucose transport

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

positive regulation of B cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.20. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleus

Inferred from direct assay Ref.20. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 15632189. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

androgen receptor binding

Inferred from direct assay Ref.20. Source: UniProtKB

calcium channel regulator activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay Ref.20. Source: UniProtKB

histone binding

Inferred from direct assay Ref.20. Source: UniProtKB

histone kinase activity (H3-T6 specific)

Inferred from direct assay Ref.20. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from mutant phenotype Ref.20. Source: UniProtKB

protein kinase C activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PHLPP1O603465EBI-5774511,EBI-2511516

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta-I (identifier: P05771-1)

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.
Isoform Beta-II (identifier: P05771-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 671670Protein kinase C beta type
PRO_0000055684

Regions

Domain173 – 26088C2
Domain342 – 600259Protein kinase
Domain601 – 67171AGC-kinase C-terminal
Zinc finger36 – 8651Phorbol-ester/DAG-type 1
Zinc finger101 – 15151Phorbol-ester/DAG-type 2
Nucleotide binding348 – 3569ATP By similarity

Sites

Active site4661Proton acceptor By similarity
Metal binding1861Calcium 1; via carbonyl oxygen By similarity
Metal binding1871Calcium 1 By similarity
Metal binding1871Calcium 2 By similarity
Metal binding1931Calcium 2 By similarity
Metal binding2461Calcium 1 By similarity
Metal binding2461Calcium 2 By similarity
Metal binding2471Calcium 2; via carbonyl oxygen By similarity
Metal binding2481Calcium 1 By similarity
Metal binding2481Calcium 2 By similarity
Metal binding2481Calcium 3 By similarity
Metal binding2511Calcium 3 By similarity
Metal binding2521Calcium 3; via carbonyl oxygen By similarity
Metal binding2541Calcium 1 By similarity
Metal binding2541Calcium 3 By similarity
Binding site3711ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue161Phosphoserine; by autocatalysis Potential
Modified residue171Phosphothreonine; by autocatalysis Potential
Modified residue2501Phosphothreonine; by autocatalysis By similarity
Modified residue3141Phosphothreonine; by autocatalysis Potential
Modified residue3241Phosphothreonine; by autocatalysis Potential
Modified residue5001Phosphothreonine; by PDPK1 Probable
Modified residue5041Phosphothreonine Ref.19
Modified residue6351Phosphothreonine; by autocatalysis
Modified residue6421Phosphothreonine Ref.24
Modified residue6611Phosphoserine; by autocatalysis Ref.24
Modified residue6621Phosphotyrosine; by SYK By similarity

Natural variations

Alternative sequence622 – 67150RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II.
VSP_004738
Natural variant1441V → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.25
VAR_042304
Natural variant4961V → M in a glioblastoma multiforme sample; somatic mutation. Ref.25
VAR_042305
Natural variant5881P → H. Ref.25
Corresponds to variant rs35631544 [ dbSNP | Ensembl ].
VAR_042306

Experimental info

Sequence conflict691V → G in CAA44393. Ref.7

Secondary structure

........................................... 671
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta-I (PRKCB1) [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 3937E7B667108C68

FASTA67176,869
        10         20         30         40         50         60 
MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF 

        70         80         90        100        110        120 
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS 

       130        140        150        160        170        180 
LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR DVLIVLVRDA 

       190        200        210        220        230        240 
KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL 

       250        260        270        280        290        300 
SVEIWDWDLT SRNDFMGSLS FGISELQKAS VDGWFKLLSQ EEGEYFNVPV PPEGSEANEE 

       310        320        330        340        350        360 
LRQKFERAKI SQGTKVPEEK TTNTVSKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE 

       370        380        390        400        410        420 
RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM 

       430        440        450        460        470        480 
EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI 

       490        500        510        520        530        540 
KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP 

       550        560        570        580        590        600 
FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF 

       610        620        630        640        650        660 
RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF 

       670 
SYTNPEFVIN V 

« Hide

Isoform Beta-II (PRKCB2) [UniParc].

Checksum: 03D42B0E4164B48F
Show »

FASTA67377,012

References

« Hide 'large scale' references
[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]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4."
Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Gunther T., Buettner R., Schule R.
Nature 464:792-796(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRKIHUC2. B24664.
KIHUC1. S00159.
RefSeqNP_002729.2. NM_002738.6.
NP_997700.1. NM_212535.2.
UniGeneHs.460355.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I0EX-ray2.60A/B321-661[»]
ProteinModelPortalP05771.
SMRP05771. Positions 37-668.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111565. 56 interactions.
DIPDIP-34187N.
IntActP05771. 12 interactions.
MINTMINT-240997.

Chemistry

BindingDBP05771.
ChEMBLCHEMBL2096620.
DrugBankDB00163. Vitamin E.
GuidetoPHARMACOLOGY1483.

PTM databases

PhosphoSiteP05771.

Polymorphism databases

DMDM20141488.

Proteomic databases

PaxDbP05771.
PRIDEP05771.

Protocols and materials databases

DNASU5579.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303531; ENSP00000305355; ENSG00000166501. [P05771-2]
ENST00000321728; ENSP00000318315; ENSG00000166501. [P05771-1]
ENST00000498058; ENSP00000454428; ENSG00000166501.
GeneID5579.
KEGGhsa:5579.
UCSCuc002dmd.3. human. [P05771-1]
uc002dme.3. human. [P05771-2]

Organism-specific databases

CTD5579.
GeneCardsGC16P023847.
HGNCHGNC:9395. PRKCB.
HPACAB003843.
MIM176970. gene.
neXtProtNX_P05771.
PharmGKBPA33761.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108317.
KOK02677.
OMAQAHIDRE.
OrthoDBEOG77M8QM.
TreeFamTF351133.

Enzyme and pathway databases

BRENDA2.7.11.13. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_13685. Neuronal System.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP05771.

Gene expression databases

ArrayExpressP05771.
BgeeP05771.
GenevestigatorP05771.

Family and domain databases

InterProIPR000961. 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]
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000550. PKC_alpha. 1 hit.
PRINTSPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSPRKCB. human.
EvolutionaryTraceP05771.
GeneWikiPRKCB1.
GenomeRNAi5579.
NextBio21632.
PMAP-CutDBP05771.
PROP05771.
SOURCESearch...

Entry information

Entry nameKPCB_HUMAN
AccessionPrimary (citable) accession number: P05771
Secondary accession number(s): C5IFJ8 expand/collapse secondary AC list , D3DWF5, O43744, P05127, Q15138, Q93060, Q9UE49, Q9UE50, Q9UEH8, Q9UJ30, Q9UJ33
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 184 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM