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UniProtKB/Swiss-Prot entry P05771


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KPCB_HUMAN
Primary accession number P05771
Secondary accession numbers O43744 P05127 Q15138 Q93060 Q9UE49 Q9UE50 Q9UEH8 Q9UJ30 Q9UJ33
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 4, 2008 (Entry version 120)
Name and origin of the protein
Protein name Protein kinase C beta type
Synonyms PKC-beta
PKC-B
EC 2.7.11.13
Gene name
Name: PRKCB1
Synonyms: PKCB, PRKCB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II).
PubMed=3755548 [NCBI, ExPASy, EBI, Israel, Japan]
Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A.;
"Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways.";
Science 233:859-866(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II).
DOI=10.1016/0014-5793(87)80524-0; PubMed=3666134 [NCBI, ExPASy, EBI, Israel, Japan]
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. 223:138-142(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1006/geno.1999.5927; PubMed=10493829 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hippocampus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
PubMed=7880442 [NCBI, ExPASy, EBI, Israel, Japan]
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. 14:213-222(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
PubMed=1556124 [NCBI, ExPASy, EBI, Israel, Japan]
Niino Y.S., Ohno S., Suzuki K.;
"Positive and negative regulation of the transcription of the human protein kinase C beta gene.";
J. Biol. Chem. 267:6158-6163(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
PubMed=1400396 [NCBI, ExPASy, EBI, Israel, Japan]
Obeid L.M., Blobe G.C., Karolak L.A., Hannun Y.A.;
"Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters.";
J. Biol. Chem. 267:20804-20810(1992).
[8]
PROTEIN SEQUENCE OF 2-19, AND ACETYLATION AT ALA-2.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-176.
Greenham J.A., Adams M.D., Doggett N.A., Mole S.E.;
"The genomic structure of the human protein kinase C beta gene (PRKCB).";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-671.
TISSUE=Fetal brain;
PubMed=3677994 [NCBI, ExPASy, EBI, Israel, Japan]
Coussens L., Rhee L., Parker P.J., Ullrich A.;
"Alternative splicing increases the diversity of the human protein kinase C family.";
DNA 6:389-394(1987).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-671.
DOI=10.1093/nar/15.17.7179; PubMed=3658678 [NCBI, ExPASy, EBI, Israel, Japan]
Kubo K., Ohno S., Suzuki K.;
"Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta-I/beta-II.";
Nucleic Acids Res. 15:7179-7180(1987).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-500 AND THR-504, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch 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 6:537-547(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-642, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 321-660 IN COMPLEX WITH INHIBITOR, AND PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
DOI=10.1021/bi061128h; PubMed=17115692 [NCBI, ExPASy, EBI, Israel, Japan]
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 45:13970-13981(2006).
[15]
VARIANTS [LARGE SCALE ANALYSIS] MET-144; MET-496 AND HIS-588.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M13975; AAA60095.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X06318; CAA29634.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07109; CAA30130.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC130454; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC002299; AAB97933.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002299; AAB97934.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036472; AAH36472.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X62532; CAA44393.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S47311; AAD13852.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D10022; BAA00912.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ002799; CAA05725.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ002800; CAA05725.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18254; AAA60096.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18255; AAA60097.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X05972; CAA29396.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X05971; CAA29395.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B24664; KIHUC2.
S00159; KIHUC1.
RefSeq NP_002729.2; -.
NP_997700.1; -.
UniGene Hs.460355
3D structure databases
PDB
2I0E; X-ray; 2.60 A; A=321-660.[ExPASy / RCSB / EBI]
PDBsum 2I0E; -.
SMR P05771; 94-158, 95-159, 156-287, 157-288, 339-668.
ModBase P05771.
Protein-protein interaction databases
IntAct P05771; -.
PTM databases
PhosphoSite P05771; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
Organism-specific databases
H-InvDB HIX0012899; -.
HGNC HGNC:9395; PRKCB1.
GenAtlas PRKCB1.
HPA CAB003843; -.
MIM 176970; gene. [NCBI / EBI]
PharmGKB PA33761; -.
GeneCards P05771.
Gene expression databases
ArrayExpress P05771; -.
GermOnline ENSG00000166501; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005886; Cellular component: plasma membrane (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004697; Molecular function: protein kinase C activity (traceable author statement from ProtInc).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (non-traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000008; C2_Ca-dep.
IPR002219; DAG_PE_bd.
IPR015745; PKC.
IPR000961; Pkinase_C.
IPR014375; Prot_kin_PKC_alpha.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
PANTHER PTHR22985:SF86; PKC; 1.
Pfam PF00130; C1_1; 2.
PF00168; C2; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000550; PKC_alpha; 1.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00109; C1; 2.
SM00239; C2; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS50004; C2; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P05771.
ProtoNet P05771.
Genome annotation databases
Ensembl ENSG00000166501; Homo sapiens. [Contig view]
GeneID 5579; -.
KEGG hsa:5579; -.
Phylogenomic databases
HOVERGEN P05771; -.
Other
DrugBank DB00163; Vitamin E.
NextBio 21632; -.
SOURCE PRKCB1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; ATP-binding; Calcium; Cytoplasm; Direct protein sequencing; Kinase; Membrane; Metal-binding; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Polymorphism; Repeat; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   671  670     Protein kinase C beta type. PRO_0000055684
DOMAIN   173   260  88     C2. 
DOMAIN   342   600  259     Protein kinase. 
DOMAIN   601   671  71     AGC-kinase C-terminal. 
ZN_FING   36    86  51     Phorbol-ester/DAG-type 1. 
ZN_FING   101   151  51     Phorbol-ester/DAG-type 2. 
NP_BIND   348   356  9     ATP (By similarity). 
ACT_SITE   466   466        Proton acceptor (By similarity). 
METAL   186   186        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   187   187        Calcium 1 (By similarity). 
METAL   187   187        Calcium 2 (By similarity). 
METAL   193   193        Calcium 2 (By similarity). 
METAL   246   246        Calcium 1 (By similarity). 
METAL   246   246        Calcium 2 (By similarity). 
METAL   247   247        Calcium 2; via carbonyl oxygen (By similarity). 
METAL   248   248        Calcium 1 (By similarity). 
METAL   248   248        Calcium 2 (By similarity). 
METAL   248   248        Calcium 3 (By similarity). 
METAL   251   251        Calcium 3 (By similarity). 
METAL   252   252        Calcium 3; via carbonyl oxygen (By similarity). 
METAL   254   254        Calcium 1 (By similarity). 
METAL   254   254        Calcium 3 (By similarity). 
BINDING   371   371        ATP (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   16    16        Phosphoserine; by autocatalysis (Potential). 
MOD_RES   17    17        Phosphothreonine; by autocatalysis (Potential). 
MOD_RES   195   195        Phosphotyrosine (By similarity). 
MOD_RES   314   314        Phosphothreonine; by autocatalysis (Potential). 
MOD_RES   324   324        Phosphothreonine; by autocatalysis (Potential). 
MOD_RES   500   500        Phosphothreonine. 
MOD_RES   504   504        Phosphothreonine. 
MOD_RES   635   635        Phosphothreonine; by autocatalysis. 
MOD_RES   642   642        Phosphothreonine. 
MOD_RES   661   661        Phosphoserine; by autocatalysis. 
VAR_SEQ   622   671        RDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFS YTNPEFVINV -> CGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS (in isoform Beta-II). VSP_004738
VARIANT   144   144  1     V -> M (in a colorectal adenocarcinoma sample; somatic mutation). VAR_042304 
VARIANT   496   496  1     V -> M (in a glioblastoma multiforme sample; somatic mutation). VAR_042305 
VARIANT   588   588  1     P -> H. VAR_042306 
CONFLICT   69    69        V -> G (in Ref. 5). 
STRAND   342   351  10      
STRAND   354   361  8      
STRAND   364   374  11      
HELIX   375   380  6      
HELIX   384   394  11      
STRAND   406   411  6      
STRAND   413   421  9      
HELIX   428   435  8      
HELIX   440   459  20      
HELIX   469   471  3      
STRAND   472   474  3      
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      
Sequence information
Length: 671 AA [This is the length of the unprocessed precursor] Molecular weight: 76869 Da [This is the MW of the unprocessed precursor] CRC64: 3937E7B667108C68 [This is a checksum on the sequence]
        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 

P05771 in FASTA format

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