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Identification
HMDB Protein ID HMDBP01372
Secondary Accession Numbers
  • 6668
Name Protein kinase C beta type
Synonyms
  1. PKC-B
  2. PKC-beta
Gene Name PRKCB
Protein Type Unknown
Biological Properties
General Function Involved in protein serine/threonine kinase activity
Specific Function Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-kappa-B activation and B-cell suvival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser- 652', leading to activate the NF-kappa-B signaling. 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. Also involved in triglyceride homeostasis. Serves as the receptor for phorbol esters, a class of tumor promoters
Pathways
  • Acrivastine H1-Antihistamine Action
  • Alcaftadine H1-Antihistamine Action
  • Alimemazine H1-Antihistamine Action
  • Antazoline H1-Antihistamine Action
  • Astemizole H1-Antihistamine Action
  • Azatadine H1-Antihistamine Action
  • Azelastine H1-Antihistamine Action
  • Bamipine H1-Antihistamine Action
  • Bepotastine H1-Antihistamine Action
  • Betahistine H1-Antihistamine Action
  • Bilastine H1-Antihistamine Action
  • Bromodiphenhydramine H1-Antihistamine Action
  • Brompheniramine H1-Antihistamine Action
  • Buclizine H1-Antihistamine Action
  • Carbinoxamine H1-Antihistamine Action
  • Cetirizine H1-Antihistamine Action
  • Chlorcyclizine H1-Antihistamine Action
  • Chloropyramine H1-Antihistamine Action
  • Chlorphenamine H1-Antihistamine Action
  • Chlorphenoxamine H1-Antihistamine Action
  • Cinnarizine H1-Antihistamine Action
  • Clemastine H1-Antihistamine Action
  • Clocinizine H1-Antihistamine Action
  • Cyclizine H1-Antihistamine Action
  • Cyproheptadine H1-Antihistamine Action
  • Deptropine H1-Antihistamine Action
  • Desloratadine H1-Antihistamine Action
  • Dexbrompheniramine H1-Antihistamine Action
  • Dexchlorpheniramine H1-Antihistamine Action
  • Dimetindene H1-Antihistamine Action
  • Diphenhydramine H1-Antihistamine Action
  • Diphenylpyraline H1-Antihistamine Action
  • Doxepin H1-Antihistamine Action
  • Doxylamine H1-Antihistamine Action
  • Ebastine H1-Antihistamine Action
  • Embramine H1-Antihistamine Action
  • Emedastine H1-Antihistamine Action
  • Epinastine H1-Antihistamine Action
  • Fenethazine H1-Antihistamine Action
  • Fexofenadine H1-Antihistamine Action
  • Flunarizine H1-Antihistamine Action
  • Histamine H1 Receptor Activation
  • Histapyrrodine H1-Antihistamine Action
  • Homochlorcyclizine H1-Antihistamine Action
  • Hydroxyethylpromethazine H1-Antihistamine Action
  • Hydroxyzine H1-Antihistamine Action
  • Isothipendyl H1-Antihistamine Action
  • Ketotifen H1-Antihistamine Action
  • Latrepirdine H1-Antihistamine Action
  • Levocabastine H1-Antihistamine Action
  • Levocetirizine H1-Antihistamine Action
  • Loratadine H1-Antihistamine Action
  • Mebhydrolin H1-Antihistamine Action
  • Meclizine H1-Antihistamine Action
  • Mepyramine H1-Antihistamine Action
  • Mequitazine H1-Antihistamine Action
  • Methapyrilene H1-Antihistamine Action
  • Methdilazine H1-Antihistamine Action
  • Mirtazapine H1-Antihistamine Action
  • Mizolastine H1-Antihistamine Action
  • Olopatadine H1-Antihistamine Action
  • Orphenadrine H1-Antihistamine Action
  • Oxatomide H1-Antihistamine Action
  • Oxomemazine H1-Antihistamine Action
  • Phenbenzamine H1-Antihistamine Action
  • Phenindamine H1-Antihistamine Action
  • Pheniramine H1-Antihistamine Action
  • Phenyltoloxamine H1-Antihistamine Action
  • Pimethixene H1-Antihistamine Action
  • Promethazine H1-Antihistamine Action
  • Propiomazine H1-Antihistamine Action
  • Pyrrobutamine H1-Antihistamine Action
  • Quetiapine H1-Antihistamine Action
  • Quifenadine H1-Antihistamine Action
  • Rupatadine H1-Antihistamine Action
  • Talastine H1-Antihistamine Action
  • Temelastine H1-Antihistamine Action
  • Terfenadine H1-Antihistamine Action
  • Thenalidine H1-Antihistamine Action
  • Thenyldiamine H1-Antihistamine Action
  • Thiazinamium H1-Antihistamine Action
  • Thonzylamine H1-Antihistamine Action
  • Tolpropamine H1-Antihistamine Action
  • Tripelennamine H1-Antihistamine Action
  • Triprolidine H1-Antihistamine Action
  • Tritoqualine H1-Antihistamine Action
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
zinc ion binding
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
protein kinase c activity
protein kinase activity
protein serine/threonine kinase activity
Process
phosphorus metabolic process
phosphate metabolic process
metabolic process
cellular metabolic process
protein amino acid phosphorylation
intracellular signaling pathway
signaling
signaling pathway
phosphorylation
Cellular Location
  1. Nucleus
  2. Cytoplasm
  3. Peripheral membrane protein
  4. Membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 16p11.2
SNPs PRKCB
Gene Sequence
>2016 bp
ATGGCTGACCCGGCTGCGGGGCCGCCGCCGAGCGAGGGCGAGGAGAGCACCGTGCGCTTC
GCCCGCAAAGGCGCCCTCCGGCAGAAGAACGTGCATGAGGTCAAGAACCACAAATTCACC
GCCCGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGCTTC
GGGAAGCAGGGATTCCAGTGCCAAGTTTGCTGCTTTGTGGTGCACAAGCGGTGCCATGAA
TTTGTCACATTCTCCTGCCCTGGCGCTGACAAGGGTCCAGCCTCCGATGACCCCCGCAGC
AAACACAAGTTTAAGATCCACACGTACTCCAGCCCCACGTTTTGTGACCACTGTGGGTCA
CTGCTGTATGGACTCATCCACCAGGGGATGAAATGTGACACCTGCATGATGAATGTGCAC
AAGCGCTGCGTGATGAATGTTCCCAGCCTGTGTGGCACGGACCACACGGAGCGCCGCGGC
CGCATCTACATCCAGGCCCACATCGACAGGGACGTCCTCATTGTCCTCGTAAGAGATGCT
AAAAACCTTGTACCTATGGACCCCAATGGCCTGTCAGATCCCTACGTAAAACTGAAACTG
ATTCCCGATCCCAAAAGTGAGAGCAAACAGAAGACCAAAACCATCAAATGCTCCCTCAAC
CCTGAGTGGAATGAGACATTTAGATTTCAGCTGAAAGAATCGGACAAAGACAGAAGACTG
TCAGTAGAGATTTGGGATTGGGATTTGACCAGCAGGAATGACTTCATGGGATCTTTGTCC
TTTGGGATTTCTGAACTTCAGAAAGCCAGTGTTGATGGCTGGTTTAAGTTACTGAGCCAG
GAGGAAGGCGAGTACTTCAATGTGCCTGTGCCACCAGAAGGAAGTGAGGCCAATGAAGAA
CTGCGGCAGAAATTTGAGAGGGCCAAGATCAGTCAGGGAACCAAGGTCCCGGAAGAAAAG
ACGACCAACACTGTCTCCAAATTTGACAACAATGGCAACAGAGACCGGATGAAACTGACC
GATTTTAACTTCCTAATGGTGCTGGGGAAAGGCAGCTTTGGCAAGGTCATGCTTTCAGAA
CGAAAAGGCACAGATGAGCTCTATGCTGTGAAGATCCTGAAGAAGGACGTTGTGATCCAA
GATGATGACGTGGAGTGCACTATGGTGGAGAAGCGGGTGTTGGCCCTGCCTGGGAAGCCG
CCCTTCCTGACCCAGCTCCACTCCTGCTTCCAGACCATGGACCGCCTGTACTTTGTGATG
GAGTACGTGAATGGGGGCGACCTCATGTATCACATCCAGCAAGTCGGCCGGTTCAAGGAG
CCCCATGCTGTATTTTACGCTGCAGAAATTGCCATCGGTCTGTTCTTCTTACAGAGTAAG
GGCATCATTTACCGTGACCTAAAACTTGACAACGTGATGCTCGATTCTGAGGGACACATC
AAGATTGCCGATTTTGGCATGTGTAAGGAAAACATCTGGGATGGGGTGACAACCAAGACA
TTCTGTGGCACTCCAGACTACATCGCCCCCGAGATAATTGCTTATCAGCCCTATGGGAAG
TCCGTGGATTGGTGGGCATTTGGAGTCCTGCTGTATGAAATGTTGGCTGGGCAGGCACCC
TTTGAAGGGGAGGATGAAGATGAACTCTTCCAATCCATCATGGAACACAACGTAGCCTAT
CCCAAGTCTATGTCCAAGGAAGCTGTGGCCATCTGCAAAGGGCTGATGACCAAACACCCA
GGCAAACGTCTGGGTTGTGGACCTGAAGGCGAACGTGATATCAAAGAGCATGCATTTTTC
CGGTATATTGATTGGGAGAAACTTGAACGCAAAGAGATCCAGCCCCCTTATAAGCCAAAA
GCTAGAGACAAGAGAGACACCTCCAACTTCGACAAAGAGTTCACCAGACAGCCTGTGGAA
CTGACCCCCACTGATAAACTCTTCATCATGAACTTGGACCAAAATGAATTTGCTGGCTTC
TCTTATACTAACCCAGAGTTTGTCATTAATGTGTAG
Protein Properties
Number of Residues 671
Molecular Weight 76868.4
Theoretical pI 7.0
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Protein kinase C beta type
MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGF
GKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGS
LLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDA
KNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRL
SVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEE
LRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSE
RKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVM
EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHI
KIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAP
FEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFF
RYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGF
SYTNPEFVINV
GenBank ID Protein 47157322
UniProtKB/Swiss-Prot ID P05771
UniProtKB/Swiss-Prot Entry Name KPCB_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_212535.2
GeneCard ID PRKCB
GenAtlas ID PRKCB
HGNC ID HGNC:9395
References
General References
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  2. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  3. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed:18088087 ]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
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  7. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed:17192257 ]
  8. Coussens L, Parker PJ, Rhee L, Yang-Feng TL, Chen E, Waterfield MD, Francke U, Ullrich A: Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways. Science. 1986 Aug 22;233(4766):859-66. [PubMed:3755548 ]
  9. Kubo K, Ohno S, Suzuki K: Primary structures of human protein kinase C beta I and beta II differ only in their C-terminal sequences. FEBS Lett. 1987 Oct 19;223(1):138-42. [PubMed:3666134 ]
  10. Mahajna J, King P, Parker P, Haley J: Autoregulation of cloned human protein kinase C beta and gamma gene promoters in U937 cells. DNA Cell Biol. 1995 Mar;14(3):213-22. [PubMed:7880442 ]
  11. Niino YS, Ohno S, Suzuki K: Positive and negative regulation of the transcription of the human protein kinase C beta gene. J Biol Chem. 1992 Mar 25;267(9):6158-63. [PubMed:1556124 ]
  12. Obeid LM, Blobe GC, Karolak LA, Hannun YA: Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters. J Biol Chem. 1992 Oct 15;267(29):20804-10. [PubMed:1400396 ]
  13. Coussens L, Rhee L, Parker PJ, Ullrich A: Alternative splicing increases the diversity of the human protein kinase C family. DNA. 1987 Oct;6(5):389-94. [PubMed:3677994 ]
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  15. Graff JR, McNulty AM, Hanna KR, Konicek BW, Lynch RL, Bailey SN, Banks C, Capen A, Goode R, Lewis JE, Sams L, Huss KL, Campbell RM, Iversen PW, Neubauer BL, Brown TJ, Musib L, Geeganage S, Thornton D: 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. Cancer Res. 2005 Aug 15;65(16):7462-9. [PubMed:16103100 ]
  16. Gao T, Brognard J, Newton AC: The phosphatase PHLPP controls the cellular levels of protein kinase C. J Biol Chem. 2008 Mar 7;283(10):6300-11. Epub 2007 Dec 27. [PubMed:18162466 ]
  17. Metzger E, Imhof A, Patel D, Kahl P, Hoffmeyer K, Friedrichs N, Muller JM, Greschik H, Kirfel J, Ji S, Kunowska N, Beisenherz-Huss C, Gunther T, Buettner R, Schule R: Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature. 2010 Apr 1;464(7289):792-6. doi: 10.1038/nature08839. Epub 2010 Mar 14. [PubMed:20228790 ]
  18. Grodsky N, Li Y, Bouzida D, Love R, Jensen J, Nodes B, Nonomiya J, Grant S: Structure of the catalytic domain of human protein kinase C beta II complexed with a bisindolylmaleimide inhibitor. Biochemistry. 2006 Nov 28;45(47):13970-81. [PubMed:17115692 ]