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Protein

Protein kinase C beta type

Gene

PRKCB

Organism
Homo sapiens (Human)
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.1 Publication

Cofactori

Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domain.By similarity

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).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi186Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi187Calcium 1By similarity1
Metal bindingi187Calcium 2By similarity1
Metal bindingi193Calcium 2By similarity1
Metal bindingi246Calcium 1By similarity1
Metal bindingi246Calcium 2By similarity1
Metal bindingi247Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi248Calcium 1By similarity1
Metal bindingi248Calcium 2By similarity1
Metal bindingi248Calcium 3By similarity1
Metal bindingi251Calcium 3By similarity1
Metal bindingi252Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi254Calcium 1By similarity1
Metal bindingi254Calcium 3By similarity1
Binding sitei371ATPPROSITE-ProRule annotation1
Active sitei466Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri36 – 86Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri101 – 151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51
Nucleotide bindingi348 – 356ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • calcium channel regulator activity Source: Ensembl
  • calcium-dependent protein kinase C activity Source: Reactome
  • chromatin binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • histone kinase activity (H3-T6 specific) Source: UniProtKB
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • protein kinase C activity Source: Reactome
  • protein kinase C binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: Reactome
  • zinc ion binding Source: InterPro

GO - Biological processi

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

Enzyme and pathway databases

BioCyciZFISH:HS09408-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-114516. Disinhibition of SNARE formation.
R-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-416993. Trafficking of GluR2-containing AMPA receptors.
R-HSA-418597. G alpha (z) signalling events.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-76005. Response to elevated platelet cytosolic Ca2+.
SABIO-RKP05771.
SignaLinkiP05771.
SIGNORiP05771.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:9395. PRKCB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5579.
OpenTargetsiENSG00000166501.
PharmGKBiPA33761.

Chemistry databases

ChEMBLiCHEMBL3045.
DrugBankiDB00675. Tamoxifen.
DB00163. Vitamin E.
GuidetoPHARMACOLOGYi1483.

Polymorphism and mutation databases

BioMutaiPRKCB.
DMDMi20141488.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000556842 – 671Protein kinase C beta typeAdd BLAST670

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei11PhosphoserineCombined sources1
Modified residuei16Phosphoserine; by autocatalysisSequence analysisBy similarity1
Modified residuei17PhosphothreonineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Modified residuei250Phosphothreonine; by autocatalysisBy similarity1
Modified residuei311PhosphoserineCombined sources1
Modified residuei314PhosphothreonineCombined sources1
Modified residuei322PhosphothreonineBy similarity1
Modified residuei324Phosphothreonine; by autocatalysisSequence analysisBy similarity1
Modified residuei500Phosphothreonine; by PDPK11 Publication1
Modified residuei504PhosphothreonineCombined sources1
Modified residuei635Phosphothreonine; by autocatalysisBy similarity1
Modified residuei642PhosphothreonineCombined sources1 Publication1
Modified residuei661Phosphoserine; by autocatalysis1 Publication1
Modified residuei662Phosphotyrosine; by SYKBy similarity1
Isoform Beta-II (identifier: P05771-2)
Modified residuei641PhosphothreonineCombined sources1
Modified residuei660PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05771.
PaxDbiP05771.
PeptideAtlasiP05771.
PRIDEiP05771.

PTM databases

iPTMnetiP05771.
PhosphoSitePlusiP05771.

Miscellaneous databases

PMAP-CutDBP05771.

Expressioni

Gene expression databases

BgeeiENSG00000166501.
ExpressionAtlasiP05771. baseline and differential.
GenevisibleiP05771. HS.

Organism-specific databases

HPAiCAB003843.
HPA048321.

Interactioni

Subunit structurei

Interacts with PDK1 (By similarity). Interacts in vitro with PRKCBP1. Interacts with PHLPP1 and PHLPP2; both proteins mediate its dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and ANDR.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PHLPP1O603465EBI-5774511,EBI-2511516
SHCBP1Q8NEM22EBI-706216,EBI-744700
TINF2Q9BSI42EBI-706216,EBI-717399

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • protein kinase C binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111565. 64 interactors.
DIPiDIP-34187N.
IntActiP05771. 22 interactors.
MINTiMINT-240997.
STRINGi9606.ENSP00000305355.

Chemistry databases

BindingDBiP05771.

Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi342 – 351Combined sources10
Beta strandi354 – 361Combined sources8
Beta strandi364 – 374Combined sources11
Helixi375 – 380Combined sources6
Helixi384 – 394Combined sources11
Beta strandi406 – 411Combined sources6
Beta strandi413 – 421Combined sources9
Helixi428 – 435Combined sources8
Helixi440 – 459Combined sources20
Helixi469 – 471Combined sources3
Beta strandi472 – 474Combined sources3
Beta strandi480 – 482Combined sources3
Helixi505 – 507Combined sources3
Helixi510 – 513Combined sources4
Helixi521 – 536Combined sources16
Helixi546 – 555Combined sources10
Helixi566 – 575Combined sources10
Helixi590 – 595Combined sources6
Helixi598 – 600Combined sources3
Helixi605 – 609Combined sources5
Helixi629 – 636Combined sources8
Turni654 – 657Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I0EX-ray2.60A/B321-671[»]
ProteinModelPortaliP05771.
SMRiP05771.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05771.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini173 – 260C2PROSITE-ProRule annotationAdd BLAST88
Domaini342 – 600Protein kinasePROSITE-ProRule annotationAdd BLAST259
Domaini601 – 671AGC-kinase C-terminalAdd BLAST71

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)DescriptionActionsGraphical viewLength
Zinc fingeri36 – 86Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri101 – 151Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST51

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOVERGENiHBG108317.
InParanoidiP05771.
KOiK19662.
OMAiQAHIDRE.
OrthoDBiEOG091G0QRS.
PhylomeDBiP05771.
TreeFamiTF351133.

Family and domain databases

CDDicd00029. C1. 2 hits.
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: P05771-1) [UniParc]FASTAAdd to basket
Also known as: PRKCB1

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 DVLIVLVRDA KNLVPMDPNG LSDPYVKLKL
210 220 230 240 250
IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL SVEIWDWDLT
260 270 280 290 300
SRNDFMGSLS FGISELQKAS VDGWFKLLSQ EEGEYFNVPV PPEGSEANEE
310 320 330 340 350
LRQKFERAKI SQGTKVPEEK TTNTVSKFDN 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):76,869
Last modified:January 23, 2007 - v4
Checksum:i3937E7B667108C68
GO
Isoform Beta-II (identifier: P05771-2) [UniParc]FASTAAdd to basket
Also known as: PRKCB2

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

Show »
Length:673
Mass (Da):77,012
Checksum:i03D42B0E4164B48F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69V → G in CAA44393 (PubMed:7880442).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042304144V → M in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs764534677dbSNPEnsembl.1
Natural variantiVAR_042305496V → M in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_042306588P → H.1 PublicationCorresponds to variant rs35631544dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_004738622 – 671RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II. 2 PublicationsAdd BLAST50

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13975 mRNA. Translation: AAA60095.1.
X06318 mRNA. Translation: CAA29634.1.
X07109 mRNA. Translation: CAA30130.1.
FJ907246 Genomic DNA. Translation: ACS14045.1.
AC130454 Genomic DNA. No translation available.
AC002299 Genomic DNA. Translation: AAB97933.1.
AC002299 Genomic DNA. Translation: AAB97934.1.
CH471145 Genomic DNA. Translation: EAW55797.1.
CH471145 Genomic DNA. Translation: EAW55798.1.
BC036472 mRNA. Translation: AAH36472.1.
X62532 Genomic DNA. Translation: CAA44393.1.
S47311 Genomic DNA. Translation: AAD13852.1.
D10022 Genomic DNA. Translation: BAA00912.1.
AJ002799, AJ002800 Genomic DNA. Translation: CAA05725.1.
M18254 Genomic DNA. Translation: AAA60096.1.
M18255 Genomic DNA. Translation: AAA60097.1.
X05972 Genomic DNA. Translation: CAA29396.1.
X05971 Genomic DNA. Translation: CAA29395.1.
CCDSiCCDS10618.1. [P05771-1]
CCDS10619.1. [P05771-2]
PIRiB24664. KIHUC2.
S00159. KIHUC1.
RefSeqiNP_002729.2. NM_002738.6. [P05771-2]
NP_997700.1. NM_212535.2. [P05771-1]
UniGeneiHs.460355.

Genome annotation databases

EnsembliENST00000303531; ENSP00000305355; ENSG00000166501. [P05771-2]
ENST00000321728; ENSP00000318315; ENSG00000166501. [P05771-1]
GeneIDi5579.
KEGGihsa:5579.
UCSCiuc002dmd.4. human. [P05771-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13975 mRNA. Translation: AAA60095.1.
X06318 mRNA. Translation: CAA29634.1.
X07109 mRNA. Translation: CAA30130.1.
FJ907246 Genomic DNA. Translation: ACS14045.1.
AC130454 Genomic DNA. No translation available.
AC002299 Genomic DNA. Translation: AAB97933.1.
AC002299 Genomic DNA. Translation: AAB97934.1.
CH471145 Genomic DNA. Translation: EAW55797.1.
CH471145 Genomic DNA. Translation: EAW55798.1.
BC036472 mRNA. Translation: AAH36472.1.
X62532 Genomic DNA. Translation: CAA44393.1.
S47311 Genomic DNA. Translation: AAD13852.1.
D10022 Genomic DNA. Translation: BAA00912.1.
AJ002799, AJ002800 Genomic DNA. Translation: CAA05725.1.
M18254 Genomic DNA. Translation: AAA60096.1.
M18255 Genomic DNA. Translation: AAA60097.1.
X05972 Genomic DNA. Translation: CAA29396.1.
X05971 Genomic DNA. Translation: CAA29395.1.
CCDSiCCDS10618.1. [P05771-1]
CCDS10619.1. [P05771-2]
PIRiB24664. KIHUC2.
S00159. KIHUC1.
RefSeqiNP_002729.2. NM_002738.6. [P05771-2]
NP_997700.1. NM_212535.2. [P05771-1]
UniGeneiHs.460355.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I0EX-ray2.60A/B321-671[»]
ProteinModelPortaliP05771.
SMRiP05771.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111565. 64 interactors.
DIPiDIP-34187N.
IntActiP05771. 22 interactors.
MINTiMINT-240997.
STRINGi9606.ENSP00000305355.

Chemistry databases

BindingDBiP05771.
ChEMBLiCHEMBL3045.
DrugBankiDB00675. Tamoxifen.
DB00163. Vitamin E.
GuidetoPHARMACOLOGYi1483.

PTM databases

iPTMnetiP05771.
PhosphoSitePlusiP05771.

Polymorphism and mutation databases

BioMutaiPRKCB.
DMDMi20141488.

Proteomic databases

MaxQBiP05771.
PaxDbiP05771.
PeptideAtlasiP05771.
PRIDEiP05771.

Protocols and materials databases

DNASUi5579.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303531; ENSP00000305355; ENSG00000166501. [P05771-2]
ENST00000321728; ENSP00000318315; ENSG00000166501. [P05771-1]
GeneIDi5579.
KEGGihsa:5579.
UCSCiuc002dmd.4. human. [P05771-1]

Organism-specific databases

CTDi5579.
DisGeNETi5579.
GeneCardsiPRKCB.
HGNCiHGNC:9395. PRKCB.
HPAiCAB003843.
HPA048321.
MIMi176970. gene.
neXtProtiNX_P05771.
OpenTargetsiENSG00000166501.
PharmGKBiPA33761.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0694. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126964.
HOVERGENiHBG108317.
InParanoidiP05771.
KOiK19662.
OMAiQAHIDRE.
OrthoDBiEOG091G0QRS.
PhylomeDBiP05771.
TreeFamiTF351133.

Enzyme and pathway databases

BioCyciZFISH:HS09408-MONOMER.
BRENDAi2.7.11.13. 2681.
ReactomeiR-HSA-114516. Disinhibition of SNARE formation.
R-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-416993. Trafficking of GluR2-containing AMPA receptors.
R-HSA-418597. G alpha (z) signalling events.
R-HSA-4419969. Depolymerisation of the Nuclear Lamina.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-76005. Response to elevated platelet cytosolic Ca2+.
SABIO-RKP05771.
SignaLinkiP05771.
SIGNORiP05771.

Miscellaneous databases

ChiTaRSiPRKCB. human.
EvolutionaryTraceiP05771.
GeneWikiiPRKCB1.
GenomeRNAii5579.
PMAP-CutDBP05771.
PROiP05771.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166501.
ExpressionAtlasiP05771. baseline and differential.
GenevisibleiP05771. HS.

Family and domain databases

CDDicd00029. C1. 2 hits.
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]
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Entry informationi

Entry nameiKPCB_HUMAN
AccessioniPrimary (citable) accession number: P05771
Secondary accession number(s): C5IFJ8
, D3DWF5, O43744, P05127, Q15138, Q93060, Q9UE49, Q9UE50, Q9UEH8, Q9UJ30, Q9UJ33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 213 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.