P05771 (KPCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	671 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 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. Ref.14 Ref.19
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.19
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.19
Subcellular location	Cytoplasm By similarity. Nucleus. Membrane; Peripheral membrane protein By similarity Ref.19.
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 process	Adaptive immunity Apoptosis Immunity Transcription Transcription regulation
Cellular component	Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding Zinc
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B 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: Compara cellular calcium ion homeostasis Inferred from electronic annotation. Source: Compara cellular response to carbohydrate stimulus Inferred from electronic annotation. Source: Compara 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 cascade 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.19. Source: UniProtKB synaptic transmission Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay Ref.19. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 15632189. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW androgen receptor binding Inferred from direct assay Ref.19. Source: UniProtKB calcium channel regulator activity Inferred from electronic annotation. Source: Compara chromatin binding Inferred from direct assay Ref.19. Source: UniProtKB histone binding Inferred from direct assay Ref.19. Source: UniProtKB histone kinase activity (H3-T6 specific) Inferred from direct assay Ref.19. Source: UniProtKB ligand-dependent nuclear receptor transcription coactivator activity Inferred from mutant phenotype Ref.19. 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...

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 671

670

Protein kinase C beta type

PRO_0000055684

Regions

Domain

173 – 260

88

C2

Domain

342 – 600

259

Protein kinase

Domain

601 – 671

71

AGC-kinase C-terminal

Zinc finger

36 – 86

51

Phorbol-ester/DAG-type 1

Zinc finger

101 – 151

51

Phorbol-ester/DAG-type 2

Nucleotide binding

348 – 356

9

ATP By similarity

Sites

Active site

466

1

Proton acceptor By similarity

Metal binding

186

1

Calcium 1; via carbonyl oxygen By similarity

Metal binding

187

1

Calcium 1 By similarity

Metal binding

187

1

Calcium 2 By similarity

Metal binding

193

1

Calcium 2 By similarity

Metal binding

246

1

Calcium 1 By similarity

Metal binding

246

1

Calcium 2 By similarity

Metal binding

247

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

248

1

Calcium 1 By similarity

Metal binding

248

1

Calcium 2 By similarity

Metal binding

248

1

Calcium 3 By similarity

Metal binding

251

1

Calcium 3 By similarity

Metal binding

252

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

254

1

Calcium 1 By similarity

Metal binding

254

1

Calcium 3 By similarity

Binding site

371

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10

Modified residue

16

1

Phosphoserine; by autocatalysis Potential

Modified residue

17

1

Phosphothreonine; by autocatalysis Potential

Modified residue

195

1

Phosphotyrosine By similarity

Modified residue

250

1

Phosphothreonine; by autocatalysis By similarity

Modified residue

314

1

Phosphothreonine; by autocatalysis Potential

Modified residue

324

1

Phosphothreonine; by autocatalysis Potential

Modified residue

500

1

Phosphothreonine; by PDPK1 Probable

Modified residue

504

1

Phosphothreonine Ref.18

Modified residue

635

1

Phosphothreonine; by autocatalysis

Modified residue

642

1

Phosphothreonine Ref.23

Modified residue

661

1

Phosphoserine; by autocatalysis Ref.23

Modified residue

662

1

Phosphotyrosine; by SYK By similarity

Natural variations

Alternative sequence

622 – 671

50

RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II.

VSP_004738

Natural variant

144

1

V → M in a colorectal adenocarcinoma sample; somatic mutation. Ref.24

VAR_042304

Natural variant

496

1

V → M in a glioblastoma multiforme sample; somatic mutation. Ref.24

VAR_042305

Natural variant

588

1

P → H. Ref.24
Corresponds to variant rs35631544 [ dbSNP | Ensembl ].

VAR_042306

Experimental info

Sequence conflict

69

1

V → G in CAA44393. Ref.7

Secondary structure

1

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671

Helix Strand Turn

Details...

Beta strand

342 – 351

10

Beta strand

354 – 361

8

Beta strand

364 – 374

11

Helix

375 – 380

6

Helix

384 – 394

11

Beta strand

406 – 411

6

Beta strand

413 – 421

9

Helix

428 – 435

8

Helix

440 – 459

20

Helix

469 – 471

3

Beta strand

472 – 474

3

Beta strand

480 – 482

3

Helix

505 – 507

3

Helix

510 – 513

4

Helix

521 – 536

16

Helix

546 – 555

10

Helix

566 – 575

10

Helix

590 – 595

6

Helix

598 – 600

3

Helix

605 – 609

5

Helix

629 – 636

8

Helix

646 – 651

6

Turn

654 – 657

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta-I (PRKCB1) [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 3937E7B667108C68	FASTA	671	76,869
	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
	Isoform Beta-II (PRKCB2) [UniParc]. Checksum: 03D42B0E4164B48F	FASTA	673	77,012
	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 ACGRNAENFD RFFTRHPPVL TPPDQEVIRN IDQSEFEGFS 670 FVNSEFLKPE VKS

References

	« Hide 'large scale' referencesShow '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. , 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]	"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), MASS SPECTROMETRY.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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].
[23]	"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.
[24]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00010466.
IPI00219628.

PIR

KIHUC2. B24664.
KIHUC1. S00159.

RefSeq

NP_002729.2. NM_002738.6.
NP_997700.1. NM_212535.2.

UniGene

Hs.460355.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2I0E	X-ray	2.60	A/B	321-661	[»]

ProteinModelPortal

P05771.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34187N.

IntAct

P05771. 6 interactions.

MINT

MINT-240997.

PTM databases

PhosphoSite

P05771.

Polymorphism databases

DMDM

20141488.

Proteomic databases

PaxDb

P05771.

PRIDE

P05771.

Protocols and materials databases

DNASU

5579.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000303531; ENSP00000305355; ENSG00000166501.
ENST00000321728; ENSP00000318315; ENSG00000166501.
ENST00000498058; ENSP00000454428; ENSG00000166501.

GeneID

5579.

KEGG

hsa:5579.

UCSC

uc002dmd.3. human.
uc002dme.3. human.

Organism-specific databases

CTD

5579.

GeneCards

GC16P023847.

HGNC

HGNC:9395. PRKCB.

HPA

CAB003843.

MIM

176970. gene.

neXtProt

NX_P05771.

PharmGKB

PA33761.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG108317.

KO

K02677.

OMA

QAHIDRE.

OrthoDB

EOG40ZQX0.

Enzyme and pathway databases

BRENDA

2.7.11.13. 2681.

Pathway_Interaction_DB

cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
endothelinpathway. Endothelins.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
il2_1pathway. IL2-mediated signaling events.
tcrjnkpathway. JNK signaling in the CD4+ TCR pathway.
tcrraspathway. Ras signaling in the CD4+ TCR pathway.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
txa2pathway. Thromboxane A2 receptor signaling.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_111102. Signal Transduction.
REACT_13685. Neuronal System.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P05771.

Bgee

P05771.

Genevestigator

P05771.

GermOnline

ENSG00000166501. Homo sapiens.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020477. C2_dom.
IPR018029. C2_membr_targeting.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_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]

Pfam

PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000550. PKC_alpha. 1 hit.

PRINTS

PR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

P05771.

ChEMBL

CHEMBL3045.

ChiTaRS

PRKCB. human.

DrugBank

DB00163. Vitamin E.

EvolutionaryTrace

P05771.

GenomeRNAi

5579.

NextBio

21632.

PMAP-CutDB

P05771.

SOURCE

Search...

Entry information

Entry name

KPCB_HUMAN

Accession

Primary (citable) accession number: P05771
Secondary accession number(s): C5IFJ8 , 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:	May 1, 2013
This is version 175 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.