Protein kinase C beta type - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P68404 (KPCB_MOUSE)

Last modified September 2, 2008. Version 54. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Protein kinase C beta type
      Short name=PKC-beta
      Short name=PKC-B
    EC=2.7.11.13

Gene names

Name:	Prkcb1
Synonyms:	Pkcb, Prkcb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	673 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (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 structure	Interacts with PDK1 By similarity.
Subcellular location	CytoplasmBy similarity. Membrane; Peripheral membrane proteinBy similarity.
Post-translational modification	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.
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.

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Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Domain	Phorbol-ester binding Repeat Zinc-finger
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	calcium ion transport Inferred from direct assay. Source: MGI cellular calcium ion homeostasis Inferred from direct assay. Source: MGI protein amino acid phosphorylation Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Inferred from direct assay. Source: MGI
Molecular function	calcium channel regulator activity Inferred from direct assay. Source: MGI protein binding Inferred from physical interaction. Source: IntAct protein kinase C activity Inferred from direct assay. Source: MGI
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BMPR2	Q13873	2	EBI-397048,EBI-527196	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 673

672

Protein kinase C beta type

Regions

Domain

173 – 260

Domain

342 – 600

259

Protein kinase

Domain

601 – 671

AGC-kinase C-terminal

Zinc finger

36 – 86

Phorbol-ester/DAG-type 1

Zinc finger

101 – 151

Phorbol-ester/DAG-type 2

Nucleotide binding

348 – 356

ATP By similarity

Sites

Active site

466

Proton acceptor By similarity

Metal binding

186

Calcium 1; via carbonyl oxygen By similarity

Metal binding

187

Calcium 1 By similarity

Metal binding

187

Calcium 2 By similarity

Metal binding

193

Calcium 2 By similarity

Metal binding

246

Calcium 1 By similarity

Metal binding

246

Calcium 2 By similarity

Metal binding

247

Calcium 2; via carbonyl oxygen By similarity

Metal binding

248

Calcium 1 By similarity

Metal binding

248

Calcium 2 By similarity

Metal binding

248

Calcium 3 By similarity

Metal binding

251

Calcium 3 By similarity

Metal binding

252

Calcium 3; via carbonyl oxygen By similarity

Metal binding

254

Calcium 1 By similarity

Metal binding

254

Calcium 3 By similarity

Binding site

371

ATP By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphoserine; by autocatalysis By similarity

Modified residue

Phosphothreonine; by autocatalysis By similarity

Modified residue

195

Phosphotyrosine

Modified residue

314

Phosphothreonine; by autocatalysis By similarity

Modified residue

324

Phosphothreonine; by autocatalysis By similarity

Modified residue

500

Phosphothreonine By similarity

Modified residue

504

Phosphothreonine By similarity

Modified residue

634

Phosphothreonine; by autocatalysis By similarity

Modified residue

641

Phosphothreonine; by autocatalysis By similarity

Modified residue

660

Phosphoserine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P68404-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A65573AAF6E224C7
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FASTA

673

76,894

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of cloned mouse protein kinase C beta-II cDNA and its sequence." Tang Y.-M., Ashendel C.L. Nucleic Acids Res. 18:5310-5310(1990) [PubMed: 2402470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ICR X Swiss Webster. Tissue: Brain.
[2]	"Protein kinase C beta controls nuclear factor kappaB activation in B cells through selective regulation of the IkappaB kinase alpha." Saijo K., Mecklenbrauker I., Santana A., Leitger M., Schmedt C., Tarakhovsky A. J. Exp. Med. 195:1647-1652(2002) [PubMed: 12070292] [Abstract] Cited for: FUNCTION.
[3]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641, MASS SPECTROMETRY. Tissue: Brain.
[4]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, MASS SPECTROMETRY. Tissue: Brain.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." 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. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X53532 mRNA. Translation: CAA37611.1.
PIR	S11213.
RefSeq	NP_032881.1.
UniGene	Mm.207496 Mm.446371
3D structure databases
SMR	P68404. Positions 94-158, 95-159, 156-287, 157-288, 339-669.
ModBase	Search...
Protein-protein interaction databases
IntAct	P68404.
Genome annotation databases
Ensembl	ENSMUSG00000052889. Mus musculus. [Contig view]
GeneID	18751.
KEGG	mmu:18751.
Organism-specific databases
MGI	MGI:97596. Prkcb1.
Phylogenomic databases
HOGENOM	P68404.
HOVERGEN	P68404.
Gene expression databases
ArrayExpress	P68404.
CleanEx	MM_PRKCB1.
GermOnline	ENSMUSG00000052889. Mus musculus.
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]
PANTHER	PTHR22985:SF86. PKC. 1 hit.
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.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00109. C1. 2 hits. SM00239. C2. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
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]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

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Entry information

Entry name

KPCB_MOUSE

Accession

Primary (citable) accession number: P68404
Secondary accession number(s): P04410, P04411

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	September 2, 2008
This is version 54 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents