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P68404 (KPCB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length671 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 p66Shcof 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. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription By similarity. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.16

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.

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) By similarity.

Subunit structure

Interacts with PDK1. Interacts in vitro with PRKCBP1. Interacts with PHLPP1 and PHLPP2; both proteins mediate its dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and ANDR By similarity. Ref.11

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Membrane; Peripheral membrane protein By similarity.

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 By similarity. Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade.

Disruption phenotype

Mice develop an immunodeficiency characterized by impaired humoral immune responses and reduced cellular responses of B-cells similar to X-linked immunodeficiency (Xid). Mice are unable to activate NF-kappa-B and promote cell survival in B-cells upon BCR signaling, or even in mast cells. B-cells fail to recruit the I-kappa-B kinase (IKK) complex into lipid rafts, activate IKK, degrade I-kappa-B or up-regulate NF-kappa-B-dependent survival signals. Moreover, mutant animals are hyperphagic and exhibit higher food intake and reduced feed efficiency versus wild type. Mice are considerably leaner and display markedly decreased size of white fat depots. Triglyceride content in the liver and skeletal muscle is also significantly low. Ref.5 Ref.8 Ref.17

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 processAdaptive immunity
Apoptosis
Immunity
Transcription
Transcription regulation
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionChromatin regulator
Kinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

B cell receptor signaling pathway

Inferred from mutant phenotype Ref.8. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion transport

Inferred from direct assay PubMed 11880265. Source: MGI

cellular calcium ion homeostasis

Inferred from direct assay PubMed 11880265. Source: MGI

cellular response to carbohydrate stimulus

Inferred from direct assay PubMed 16585392. Source: MGI

histone H3-T6 phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

negative regulation of glucose transport

Inferred from mutant phenotype Ref.6. Source: UniProtKB

negative regulation of insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of B cell receptor signaling pathway

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype Ref.8. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.9. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 12618484PubMed 15545601. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12826667PubMed 14613966. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

androgen receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

calcium channel regulator activity

Inferred from direct assay PubMed 11880265. Source: MGI

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone kinase activity (H3-T6 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase C activity

Inferred from direct assay PubMed 12618484PubMed 15545601. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BMPR2Q138734EBI-397048,EBI-527196From a different organism.
EIF6P565372EBI-397048,EBI-372243From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta-I (identifier: P68404-1)

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: P68404-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 671670Protein kinase C beta type
PRO_0000055685

Regions

Domain173 – 26088C2
Domain342 – 600259Protein kinase
Domain601 – 67171AGC-kinase C-terminal
Zinc finger36 – 8651Phorbol-ester/DAG-type 1
Zinc finger101 – 15151Phorbol-ester/DAG-type 2
Nucleotide binding348 – 3569ATP By similarity

Sites

Active site4661Proton acceptor By similarity
Metal binding1861Calcium 1; via carbonyl oxygen By similarity
Metal binding1871Calcium 1 By similarity
Metal binding1871Calcium 2 By similarity
Metal binding1931Calcium 2 By similarity
Metal binding2461Calcium 1 By similarity
Metal binding2461Calcium 2 By similarity
Metal binding2471Calcium 2; via carbonyl oxygen By similarity
Metal binding2481Calcium 1 By similarity
Metal binding2481Calcium 2 By similarity
Metal binding2481Calcium 3 By similarity
Metal binding2511Calcium 3 By similarity
Metal binding2521Calcium 3; via carbonyl oxygen By similarity
Metal binding2541Calcium 1 By similarity
Metal binding2541Calcium 3 By similarity
Binding site3711ATP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue161Phosphoserine; by autocatalysis By similarity
Modified residue171Phosphothreonine; by autocatalysis By similarity
Modified residue2501Phosphothreonine; by autocatalysis By similarity
Modified residue3141Phosphothreonine; by autocatalysis By similarity
Modified residue3241Phosphothreonine; by autocatalysis By similarity
Modified residue5001Phosphothreonine; by PDPK1 By similarity
Modified residue5041Phosphothreonine By similarity
Modified residue6351Phosphothreonine; by autocatalysis By similarity
Modified residue6421Phosphothreonine; by autocatalysis By similarity
Modified residue6611Phosphoserine By similarity
Modified residue6621Phosphotyrosine; by SYK Ref.10

Natural variations

Alternative sequence622 – 67150RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II.
VSP_041812

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta-I [UniParc].

Last modified September 21, 2011. Version 4.
Checksum: A1935030F758513C

FASTA67176,751
        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 ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF 

       670 
SYTNPEFVIN V 

« Hide

Isoform Beta-II [UniParc].

Checksum: A65573AAF6E224C7
Show »

FASTA67376,894

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-I).
Strain: ICR X Swiss Webster.
Tissue: Brain.
[2]"Nucleotide sequence of cDNA for mouse brain protein kinase C beta-I subspecies."
Powell C.T.
Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II).
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] (ISOFORMS BETA-I).
[5]"Immunodeficiency in protein kinase cbeta-deficient mice."
Leitges M., Schmedt C., Guinamard R., Davoust J., Schaal S., Stabel S., Tarakhovsky A.
Science 273:788-791(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Effects of knockout of the protein kinase C beta gene on glucose transport and glucose homeostasis."
Standaert M.L., Bandyopadhyay G., Galloway L., Soto J., Ono Y., Kikkawa U., Farese R.V., Leitges M.
Endocrinology 140:4470-4477(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INSULIN SIGNALING.
[7]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"PKC-beta controls I kappa B kinase lipid raft recruitment and activation in response to BCR signaling."
Su T.T., Guo B., Kawakami Y., Sommer K., Chae K., Humphries L.A., Kato R.M., Kang S., Patrone L., Wall R., Teitell M., Leitges M., Kawakami T., Rawlings D.J.
Nat. Immunol. 3:780-786(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"Characterization of protein kinase C beta isoform's action on retinoblastoma protein phosphorylation, vascular endothelial growth factor-induced endothelial cell proliferation, and retinal neovascularization."
Suzuma K., Takahara N., Suzuma I., Isshiki K., Ueki K., Leitges M., Aiello L.P., King G.L.
Proc. Natl. Acad. Sci. U.S.A. 99:721-726(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOTHELIAL CELLS PROLIFERATION.
[10]"A Ras activation pathway dependent on Syk phosphorylation of protein kinase C."
Kawakami Y., Kitaura J., Yao L., McHenry R.W., Kawakami Y., Newton A.C., Kang S., Kato R.M., Leitges M., Rawlings D.J., Kawakami T.
Proc. Natl. Acad. Sci. U.S.A. 100:9470-9475(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-662.
[11]"Phosphorylation of the CARMA1 linker controls NF-kappaB activation."
Sommer K., Guo B., Pomerantz J.L., Bandaranayake A.D., Moreno-Garcia M.E., Ovechkina Y.L., Rawlings D.J.
Immunity 23:561-574(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CARD11.
[12]"PKC beta regulates BCR-mediated IKK activation by facilitating the interaction between TAK1 and CARMA1."
Shinohara H., Yasuda T., Aiba Y., Sanjo H., Hamadate M., Watarai H., Sakurai H., Kurosaki T.
J. Exp. Med. 202:1423-1431(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION.
[13]"Activation of vascular protein kinase C-beta inhibits Akt-dependent endothelial nitric oxide synthase function in obesity-associated insulin resistance."
Naruse K., Rask-Madsen C., Takahara N., Ha S.W., Suzuma K., Way K.J., Jacobs J.R., Clermont A.C., Ueki K., Ohshiro Y., Zhang J., Goldfine A.B., King G.L.
Diabetes 55:691-698(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOTHELIAL CELLS.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641 (ISOFORM BETA-II), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[15]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[16]"Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc."
Pinton P., Rimessi A., Marchi S., Orsini F., Migliaccio E., Giorgio M., Contursi C., Minucci S., Mantovani F., Wieckowski M.R., Del Sal G., Pelicci P.G., Rizzuto R.
Science 315:659-663(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Protein kinase C deficiency increases fatty acid oxidation and reduces fat storage."
Bansode R.R., Huang W., Roy S.K., Mehta M., Mehta K.D.
J. Biol. Chem. 283:231-236(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53532 mRNA. Translation: CAA37611.1.
X59274 mRNA. No translation available.
AC016522 Genomic DNA. No translation available.
AC122232 Genomic DNA. No translation available.
AC123837 Genomic DNA. No translation available.
AC151986 Genomic DNA. No translation available.
BC127083 mRNA. Translation: AAI27084.1.
PIRS11213.
RefSeqNP_032881.1. NM_008855.2.
XP_006507505.1. XM_006507442.1.
UniGeneMm.207496.
Mm.446371.

3D structure databases

ProteinModelPortalP68404.
SMRP68404. Positions 37-668.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202195. 8 interactions.
DIPDIP-31583N.
IntActP68404. 6 interactions.
MINTMINT-98059.

Chemistry

BindingDBP68404.

PTM databases

PhosphoSiteP68404.

Proteomic databases

PaxDbP68404.
PRIDEP68404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064921; ENSMUSP00000064812; ENSMUSG00000052889. [P68404-1]
ENSMUST00000064989; ENSMUSP00000070019; ENSMUSG00000052889. [P68404-2]
ENSMUST00000143692; ENSMUSP00000138788; ENSMUSG00000052889. [P68404-2]
GeneID18751.
KEGGmmu:18751.
UCSCuc009jot.1. mouse. [P68404-1]
uc009jou.1. mouse. [P68404-2]

Organism-specific databases

CTD5579.
MGIMGI:97596. Prkcb.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117339.
HOGENOMHOG000233022.
HOVERGENHBG108317.
InParanoidA0JNZ5.
KOK02677.
OMAQAHIDRE.
OrthoDBEOG77M8QM.
TreeFamTF351133.

Gene expression databases

BgeeP68404.
GenevestigatorP68404.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_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]
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000550. PKC_alpha. 1 hit.
PRINTSPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSPRKCB. mouse.
NextBio294921.
PROP68404.
SOURCESearch...

Entry information

Entry nameKPCB_MOUSE
AccessionPrimary (citable) accession number: P68404
Secondary accession number(s): A0JNZ5 expand/collapse secondary AC list , F2Z441, P04410, P04411
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 112 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

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