Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein kinase C beta type

Gene

Prkcb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 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. 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 (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.By similarity3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Ca2+2 PublicationsNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domain.2 Publications

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi186 – 1861Calcium 1; via carbonyl oxygen2 Publications
Metal bindingi187 – 1871Calcium 12 Publications
Metal bindingi187 – 1871Calcium 22 Publications
Metal bindingi193 – 1931Calcium 22 Publications
Metal bindingi246 – 2461Calcium 12 Publications
Metal bindingi246 – 2461Calcium 22 Publications
Metal bindingi247 – 2471Calcium 2; via carbonyl oxygen2 Publications
Metal bindingi248 – 2481Calcium 12 Publications
Metal bindingi248 – 2481Calcium 22 Publications
Metal bindingi248 – 2481Calcium 32 Publications
Metal bindingi251 – 2511Calcium 32 Publications
Metal bindingi252 – 2521Calcium 3; via carbonyl oxygen2 Publications
Metal bindingi254 – 2541Calcium 12 Publications
Metal bindingi254 – 2541Calcium 32 Publications
Binding sitei371 – 3711ATPPROSITE-ProRule annotation
Active sitei466 – 4661Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 8651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri101 – 15151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi348 – 3569ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • apoptotic process Source: UniProtKB-KW
  • B cell activation Source: UniProtKB
  • B cell receptor signaling pathway Source: UniProtKB
  • dibenzo-p-dioxin metabolic process Source: RGD
  • histone H3-T6 phosphorylation Source: UniProtKB
  • intracellular signal transduction Source: RGD
  • negative regulation of glucose transport Source: UniProtKB
  • negative regulation of insulin receptor signaling pathway Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of B cell receptor signaling pathway Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of odontogenesis of dentin-containing tooth Source: RGD
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  • regulation of dopamine secretion Source: RGD
  • regulation of growth Source: RGD
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to glucose Source: RGD
  • response to vitamin D Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Adaptive immunity, Apoptosis, Immunity, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C beta type (EC:2.7.11.13)
Short name:
PKC-B
Short name:
PKC-beta
Gene namesi
Name:Prkcb
Synonyms:Pkcb, Prkcb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3396. Prkcb.

Subcellular locationi

GO - Cellular componenti

  • brush border membrane Source: RGD
  • centrosome Source: RGD
  • cytosol Source: RGD
  • nucleus Source: UniProtKB
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 172ST → AA: No effect. 1 Publication
Mutagenesisi314 – 3141T → A: No effect; when associated with A-323. 1 Publication
Mutagenesisi324 – 3241T → A: No effect; when associated with A-313. 1 Publication
Mutagenesisi500 – 5001T → E: 50% increase of enzymatic activity. 1 Publication
Mutagenesisi500 – 5001T → S: 50% decrease of enzymatic activity. 1 Publication
Mutagenesisi500 – 5001T → V or D: Loss of enzymatic activity. 1 Publication
Mutagenesisi635 – 6351T → A: Loss of enzymatic activity; when associated with T-643 change in subcellular location, loss of PMA-induced down-regulation and loss of enzymatic activity. 2 Publications
Mutagenesisi642 – 6421T → A: Loss of enzymatic activity; when associated with T-636 change in subcellular location, loss of PMA-induced down-regulation and loss of enzymatic activity. 2 Publications

Chemistry

ChEMBLiCHEMBL2097168.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 671670Protein kinase C beta typePRO_0000055687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei16 – 161Phosphoserine; by autocatalysis1 Publication
Modified residuei17 – 171Phosphothreonine; by autocatalysis1 Publication
Modified residuei250 – 2501Phosphothreonine; by autocatalysisBy similarity
Modified residuei314 – 3141Phosphothreonine; by autocatalysis1 Publication
Modified residuei324 – 3241Phosphothreonine; by autocatalysis1 Publication
Modified residuei500 – 5001Phosphothreonine; by PDPK13 Publications
Modified residuei504 – 5041PhosphothreonineBy similarity
Modified residuei635 – 6351Phosphothreonine; by autocatalysis1 Publication
Modified residuei642 – 6421Phosphothreonine; by autocatalysis3 Publications
Modified residuei661 – 6611Phosphoserine; by autocatalysis2 Publications
Modified residuei662 – 6621Phosphotyrosine; by SYKBy similarity
Isoform Beta-II (identifier: P68403-2)
Modified residuei641 – 6411PhosphothreonineCombined sources
Modified residuei654 – 6541PhosphoserineCombined sources
Modified residuei660 – 6601PhosphoserineCombined sources
Modified residuei664 – 6641PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation on Thr-500 of isoform beta-I, 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. Similarly, isoform beta-II is autophosphorylated on 'Thr-641' and 'Ser-660', subsequent to phosphorylation on Thr-500. Autophosphorylated on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP68403.
PRIDEiP68403.

PTM databases

iPTMnetiP68403.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PtpraP180523EBI-397072,EBI-6597520From a different organism.
TRIM41Q8WV44-23EBI-397092,EBI-726015From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi247103. 11 interactions.
IntActiP68403. 4 interactions.
MINTiMINT-4099933.
STRINGi10116.ENSRNOP00000016417.

Chemistry

BindingDBiP68403.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi161 – 18222Combined sources
Beta strandi194 – 2029Combined sources
Beta strandi222 – 2309Combined sources
Helixi234 – 2374Combined sources
Beta strandi239 – 2468Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi254 – 2629Combined sources
Helixi263 – 2664Combined sources
Beta strandi271 – 2766Combined sources
Helixi280 – 2834Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A25X-ray2.70A/B154-289[»]
3PFQX-ray4.00A1-661[»]
ProteinModelPortaliP68403.
SMRiP68403. Positions 37-668.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68403.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini173 – 26088C2PROSITE-ProRule annotationAdd
BLAST
Domaini342 – 600259Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini601 – 67171AGC-kinase C-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri36 – 8651Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri101 – 15151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP68403.
KOiK19662.
PhylomeDBiP68403.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Beta-I (identifier: P68403-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC
60 70 80 90 100
SHCTDFIWGF GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS
110 120 130 140 150
KHKFKIHTYS SPTFCDHCGS LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL
160 170 180 190 200
CGTDHTERRG RIYIQAHIDR EVLIVVVRDA KNLVPMDPNG LSDPYVKLKL
210 220 230 240 250
IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL SVEIWDWDLT
260 270 280 290 300
SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE
310 320 330 340 350
LRQKFERAKI GQGTKAPEEK TANTISKFDN NGNRDRMKLT DFNFLMVLGK
360 370 380 390 400
GSFGKVMLSE RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP
410 420 430 440 450
PFLTQLHSCF QTMDRLYFVM EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI
460 470 480 490 500
AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI KIADFGMCKE NIWDGVTTKT
510 520 530 540 550
FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP FEGEDEDELF
560 570 580 590 600
QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF
610 620 630 640 650
RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM
660 670
NLDQNEFAGF SYTNPEFVIN V
Length:671
Mass (Da):76,751
Last modified:January 23, 2007 - v3
Checksum:iA1935030F758513C
GO
Isoform Beta-II (identifier: P68403-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     622-671: RDKRDTSNFD...YTNPEFVINV → CGRNAENFDR...SEFLKPEVKS

Show »
Length:673
Mass (Da):76,894
Checksum:iA65573AAF6E224C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251A → P in AAA41868 (PubMed:3345563).Curated
Sequence conflicti126 – 1261I → V in AAA41875 (PubMed:3755379).Curated
Sequence conflicti138 – 1381N → S in AAA41875 (PubMed:3755379).Curated
Sequence conflicti141 – 1411K → R in AAA41875 (PubMed:3755379).Curated
Sequence conflicti149 – 1491S → G in AAA41875 (PubMed:3755379).Curated
Sequence conflicti164 – 1641I → V in AAA41875 (PubMed:3755379).Curated
Sequence conflicti170 – 1712RE → GG in AAA41875 (PubMed:3755379).Curated
Sequence conflicti174 – 1741I → V in AAA41875 (PubMed:3755379).Curated
Sequence conflicti294 – 2941G → E in AAA41868 (PubMed:3345563).Curated
Sequence conflicti419 – 4191V → M in CAA28035 (PubMed:2428667).Curated
Sequence conflicti419 – 4191V → M in CAA28036 (PubMed:2428667).Curated
Sequence conflicti628 – 6281Missing in AAA41865 (PubMed:3755379).Curated
Sequence conflicti640 – 6401Missing in AAA41865 (PubMed:3755379).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei622 – 67150RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II. 2 PublicationsVSP_004739Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13706 mRNA. Translation: AAA41875.1.
K03485 mRNA. Translation: AAA41864.1.
K03486 mRNA. Translation: AAA41865.1.
X04439 Genomic DNA. Translation: CAA28035.1.
X04440 mRNA. Translation: CAA28036.1.
M19007 mRNA. Translation: AAA41868.1.
X04139 mRNA. Translation: CAA27756.1.
M15522 mRNA. Translation: AAA41876.1.
PIRiA00622. KIRTC1.
RefSeqiNP_001165776.1. NM_001172305.1.
NP_036845.3. NM_012713.3.
UniGeneiRn.91118.

Genome annotation databases

GeneIDi25023.
KEGGirno:25023.
UCSCiRGD:3396. rat.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13706 mRNA. Translation: AAA41875.1.
K03485 mRNA. Translation: AAA41864.1.
K03486 mRNA. Translation: AAA41865.1.
X04439 Genomic DNA. Translation: CAA28035.1.
X04440 mRNA. Translation: CAA28036.1.
M19007 mRNA. Translation: AAA41868.1.
X04139 mRNA. Translation: CAA27756.1.
M15522 mRNA. Translation: AAA41876.1.
PIRiA00622. KIRTC1.
RefSeqiNP_001165776.1. NM_001172305.1.
NP_036845.3. NM_012713.3.
UniGeneiRn.91118.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A25X-ray2.70A/B154-289[»]
3PFQX-ray4.00A1-661[»]
ProteinModelPortaliP68403.
SMRiP68403. Positions 37-668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247103. 11 interactions.
IntActiP68403. 4 interactions.
MINTiMINT-4099933.
STRINGi10116.ENSRNOP00000016417.

Chemistry

BindingDBiP68403.
ChEMBLiCHEMBL2097168.

PTM databases

iPTMnetiP68403.

Proteomic databases

PaxDbiP68403.
PRIDEiP68403.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25023.
KEGGirno:25023.
UCSCiRGD:3396. rat.

Organism-specific databases

CTDi5579.
RGDi3396. Prkcb.

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
HOGENOMiHOG000233022.
HOVERGENiHBG108317.
InParanoidiP68403.
KOiK19662.
PhylomeDBiP68403.

Miscellaneous databases

EvolutionaryTraceiP68403.
NextBioi294921.
PROiP68403.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000008. C2_dom.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. PE/DAG-bd.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000550. PKC_alpha. 1 hit.
PRINTSiPR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of multiple protein kinase C cDNAs."
    Knopf J.L., Lee M.-H., Sultzman L.A., Kriz R.W., Loomis C.R., Hewick R.M., Bell R.M.
    Cell 46:491-502(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II).
  2. "Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing."
    Ono Y., Kurokawa T., Fujii T., Kawahara K., Igarashi K., Kikkawa U., Ogita K., Nishizuka Y.
    FEBS Lett. 206:347-352(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS BETA-I AND BETA-II).
    Tissue: Brain.
  3. "Overproduction of protein kinase C causes disordered growth control in rat fibroblasts."
    Housey G.M., Johnson M.D., Hsiao W.L.W., O'Brian C.A., Murphy J.P., Kirschmeier P., Weinstein I.B.
    Cell 52:343-354(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-I).
    Tissue: Fibroblast.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 448-671 (ISOFORM BETA-I).
  5. "Isolation of cDNA clones encoding protein kinase C: evidence for a protein kinase C-related gene family."
    Housey G.M., O'Brian C.A., Johnson M.D., Kirschmeier P., Weinstein I.B.
    Proc. Natl. Acad. Sci. U.S.A. 84:1065-1069(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 448-671 (ISOFORM BETA-I).
  6. "Protein kinase C is regulated in vivo by three functionally distinct phosphorylations."
    Keranen L.M., Dutil E.M., Newton A.C.
    Curr. Biol. 5:1394-1403(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 500-520 AND 636-663 (ISOFORM BETA-II), PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
  7. "Characterization of site-specific mutants altered at protein kinase C beta 1 isozyme autophosphorylation sites."
    Zhang J., Wang L., Petrin J., Bishop W.R., Bond R.W.
    Proc. Natl. Acad. Sci. U.S.A. 90:6130-6134(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-16; THR-17; THR-314; THR-324; THR-635 AND THR-642, MUTAGENESIS OF 16-SER-THR-17; THR-314; THR-324; THR-635 AND THR-642.
  8. "Phosphorylation of Thr642 is an early event in the processing of newly synthesized protein kinase C beta 1 and is essential for its activation."
    Zhang J., Wang L., Schwartz J., Bond R.W., Bishop W.R.
    J. Biol. Chem. 269:19578-19584(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-642 (ISOFORM BETA-I), MUTAGENESIS OF THR-635 AND THR-642.
  9. "Requirement for negative charge on 'activation loop' of protein kinase C."
    Orr J.W., Newton A.C.
    J. Biol. Chem. 269:27715-27718(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-500, MUTAGENESIS OF THR-500.
  10. "Insulin-activated protein kinase Cbeta bypasses Ras and stimulates mitogen-activated protein kinase activity and cell proliferation in muscle cells."
    Formisano P., Oriente F., Fiory F., Caruso M., Miele C., Maitan M.A., Andreozzi F., Vigliotta G., Condorelli G., Beguinot F.
    Mol. Cell. Biol. 20:6323-6333(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INSULIN SIGNALING.
  11. "Involvement of protein kinase C beta 2 in c-myc induction by high glucose in pancreatic beta-cells."
    Kaneto H., Suzuma K., Sharma A., Bonner-Weir S., King G.L., Weir G.C.
    J. Biol. Chem. 277:3680-3685(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INSULIN SIGNALING.
  12. "Phosphorylation of activation transcription factor-2 at serine 121 by protein kinase c controls c-Jun-mediated activation of transcription."
    Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.
    J. Biol. Chem. 284:8567-8581(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641; SER-654; SER-660 AND SER-664 (ISOFORM BETA-II), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+."
    Sutton R.B., Sprang S.R.
    Structure 6:1395-1405(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 157-288 IN COMPLEX WITH CALCIUM IONS, COFACTOR.
  15. "Crystal structure and allosteric activation of protein kinase C betaII."
    Leonard T.A., Rozycki B., Saidi L.F., Hummer G., Hurley J.H.
    Cell 144:55-66(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 1-661 IN COMPLEX WITH CALCIUM IONS, COFACTOR, PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.

Entry informationi

Entry nameiKPCB_RAT
AccessioniPrimary (citable) accession number: P68403
Secondary accession number(s): P04410, P04411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.