[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=ICR X Swiss Webster; TISSUE=Brain; DOI=10.1093/nar/18.17.5310; PubMed=2402470 [NCBI, ExPASy, EBI, Israel, Japan] Tang Y.-M., Ashendel C.L.; "Isolation of cloned mouse protein kinase C beta-II cDNA and its sequence."; Nucleic Acids Res. 18:5310-5310(1990).
[2]	FUNCTION. DOI=10.1084/jem.20020408; PubMed=12070292 [NCBI, ExPASy, EBI, Israel, Japan] Saijo K., Mecklenbrauker I., Santana A., Leitger M., Schmedt C., Tarakhovsky A.; "Protein kinase C beta controls nuclear factor kappaB activation in B cells through selective regulation of the IkappaB kinase alpha."; J. Exp. Med. 195:1647-1652(2002).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1074/mcp.T500041-MCP200; PubMed=16452087 [NCBI, ExPASy, EBI, Israel, Japan] Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."; Mol. Cell. Proteomics 5:914-922(2006).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan] Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."; J. Proteome Res. 7:311-318(2008).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641, AND MASS SPECTROMETRY. TISSUE=Brain cortex; DOI=10.1074/mcp.M600046-MCP200; PubMed=17114649 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."; Mol. Cell. Proteomics 6:283-293(2007).

Comments

FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to the C2 domain (By similarity).
SUBUNIT: Interacts with PDK1 (By similarity).
INTERACTION:
Q13873:BMPR2 (xeno); NbExp=2; IntAct=EBI-397048, EBI-527196;
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; Peripheral membrane protein (By similarity).
PTM: Phosphorylation on Thr-500 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-641 maintains catalytic competence, and autophosphorylation on Ser-660 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).
SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
SIMILARITY: Contains 1 C2 domain.
SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
SIMILARITY: Contains 1 protein kinase domain.

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

X53532; CAA37611.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S11213; S11213.

NP_032881.1; -.

3D structure databases

SMR

P68404; 94-158, 95-159, 156-287, 157-288, 339-669.

ModBase

P68404.

Protein-protein interaction databases

IntAct

P68404; -.

Organism-specific databases

MGI

MGI:97596; Prkcb.

Gene expression databases

ArrayExpress

P68404; -.

CleanEx

MM_PRKCB1; -.

GermOnline

ENSMUSG00000052889; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from MGI).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005246;	Molecular function: calcium channel regulator activity (inferred from direct assay from MGI).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019992;	Molecular function: diacylglycerol binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004697;	Molecular function: protein kinase C activity (inferred from direct assay from MGI).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006816;	Biological process: calcium ion transport (inferred from direct assay from MGI).
GO:0006874;	Biological process: cellular calcium ion homeostasis (inferred from direct assay from MGI).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from direct assay from MGI).
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).

ProtoNet

P68404.

Genome annotation databases

Ensembl

ENSMUSG00000052889; Mus musculus. [Contig view]

GeneID

18751; -.

KEGG

mmu:18751; -.

Phylogenomic databases

HOGENOM

P68404; -.

HOVERGEN

P68404; -.

Other

NextBio

294921; -.

SOURCE

Prkcb; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; ATP-binding; Calcium; Cytoplasm; Kinase; Membrane; Metal-binding; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 673`	`672`	`Protein kinase C beta type.`	`PRO_0000055685`
`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 (By similarity).`
`MOD_RES`	`16 16`		`Phosphoserine; by autocatalysis (By similarity).`
`MOD_RES`	`17 17`		`Phosphothreonine; by autocatalysis (By similarity).`
`MOD_RES`	`195 195`		`Phosphotyrosine.`
`MOD_RES`	`314 314`		`Phosphothreonine; by autocatalysis (By similarity).`
`MOD_RES`	`324 324`		`Phosphothreonine; by autocatalysis (By similarity).`
`MOD_RES`	`500 500`		`Phosphothreonine (By similarity).`
`MOD_RES`	`504 504`		`Phosphothreonine (By similarity).`
`MOD_RES`	`634 634`		`Phosphothreonine; by autocatalysis (By similarity).`
`MOD_RES`	`641 641`		`Phosphothreonine; by autocatalysis (By similarity).`
`MOD_RES`	`660 660`		`Phosphoserine (By similarity).`

Sequence information

Length: 673 AA [This is the length of the unprocessed precursor]

Molecular weight: 76894 Da [This is the MW of the unprocessed precursor]

CRC64: A65573AAF6E224C7 [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 EVLIVVVRDA 

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

       250        260        270        280        290        300 
SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE 

       310        320        330        340        350        360 
LRQKFERAKI GQGTKAPEEK TANTISKFDN 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

P68404 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools