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P05771

- KPCB_HUMAN

UniProt

P05771 - KPCB_HUMAN

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Protein

Protein kinase C beta type

Gene

PRKCB

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 3 calcium ions per subunit. The ions are bound to the C2 domain (By similarity).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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi186 – 1861Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi187 – 1871Calcium 1By similarity
Metal bindingi187 – 1871Calcium 2By similarity
Metal bindingi193 – 1931Calcium 2By similarity
Metal bindingi246 – 2461Calcium 1By similarity
Metal bindingi246 – 2461Calcium 2By similarity
Metal bindingi247 – 2471Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi248 – 2481Calcium 1By similarity
Metal bindingi248 – 2481Calcium 2By similarity
Metal bindingi248 – 2481Calcium 3By similarity
Metal bindingi251 – 2511Calcium 3By similarity
Metal bindingi252 – 2521Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi254 – 2541Calcium 1By similarity
Metal bindingi254 – 2541Calcium 3By similarity
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

  1. androgen receptor binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. calcium channel regulator activity Source: Ensembl
  4. chromatin binding Source: UniProtKB
  5. histone binding Source: UniProtKB
  6. histone kinase activity (H3-T6 specific) Source: UniProtKB
  7. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  8. protein kinase C activity Source: ProtInc
  9. protein kinase C binding Source: UniProtKB
  10. protein serine/threonine kinase activity Source: Reactome
  11. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. B cell activation Source: UniProtKB
  3. B cell receptor signaling pathway Source: UniProtKB
  4. blood coagulation Source: Reactome
  5. calcium ion transport Source: Ensembl
  6. cellular calcium ion homeostasis Source: Ensembl
  7. cellular response to carbohydrate stimulus Source: Ensembl
  8. histone H3-T6 phosphorylation Source: UniProtKB
  9. intracellular signal transduction Source: InterPro
  10. lipoprotein transport Source: BHF-UCL
  11. negative regulation of glucose transport Source: UniProtKB
  12. negative regulation of insulin receptor signaling pathway Source: UniProtKB
  13. platelet activation Source: Reactome
  14. positive regulation of angiogenesis Source: UniProtKB
  15. positive regulation of B cell receptor signaling pathway Source: UniProtKB
  16. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  17. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  18. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  19. protein phosphorylation Source: ProtInc
  20. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  21. signal transduction Source: ProtInc
  22. synaptic transmission Source: Reactome
  23. 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

Enzyme and pathway databases

BRENDAi2.7.11.13. 2681.
ReactomeiREACT_1178. Disinhibition of SNARE formation.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1280. Response to elevated platelet cytosolic Ca2+.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_19333. G alpha (z) signalling events.
REACT_200828. Depolymerisation of the Nuclear Lamina.
SignaLinkiP05771.

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
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:9395. PRKCB.

Subcellular locationi

Cytoplasm By similarity. Nucleus 1 Publication. Membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33761.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 671670Protein kinase C beta typePRO_0000055684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei16 – 161Phosphoserine; by autocatalysisSequence Analysis
Modified residuei17 – 171Phosphothreonine; by autocatalysisSequence Analysis
Modified residuei250 – 2501Phosphothreonine; by autocatalysisBy similarity
Modified residuei314 – 3141Phosphothreonine; by autocatalysisSequence Analysis
Modified residuei324 – 3241Phosphothreonine; by autocatalysisSequence Analysis
Modified residuei500 – 5001Phosphothreonine; by PDPK11 Publication
Modified residuei504 – 5041Phosphothreonine1 Publication
Modified residuei635 – 6351Phosphothreonine; by autocatalysis
Modified residuei642 – 6421Phosphothreonine1 Publication
Modified residuei661 – 6611Phosphoserine; by autocatalysis1 Publication
Modified residuei662 – 6621Phosphotyrosine; by SYKBy similarity

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.
PRIDEiP05771.

PTM databases

PhosphoSiteiP05771.

Miscellaneous databases

PMAP-CutDBP05771.

Expressioni

Gene expression databases

BgeeiP05771.
ExpressionAtlasiP05771. baseline and differential.
GenevestigatoriP05771.

Organism-specific databases

HPAiCAB003843.

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

Protein-protein interaction databases

BioGridi111565. 57 interactions.
DIPiDIP-34187N.
IntActiP05771. 18 interactions.
MINTiMINT-240997.

Structurei

Secondary structure

1
671
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi342 – 35110
Beta strandi354 – 3618
Beta strandi364 – 37411
Helixi375 – 3806
Helixi384 – 39411
Beta strandi406 – 4116
Beta strandi413 – 4219
Helixi428 – 4358
Helixi440 – 45920
Helixi469 – 4713
Beta strandi472 – 4743
Beta strandi480 – 4823
Helixi505 – 5073
Helixi510 – 5134
Helixi521 – 53616
Helixi546 – 55510
Helixi566 – 57510
Helixi590 – 5956
Helixi598 – 6003
Helixi605 – 6095
Helixi629 – 6368
Turni654 – 6574

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I0EX-ray2.60A/B321-671[»]
ProteinModelPortaliP05771.
SMRiP05771. Positions 37-668.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05771.

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

eggNOGiCOG0515.
GeneTreeiENSGT00760000118891.
HOVERGENiHBG108317.
InParanoidiP05771.
KOiK02677.
OMAiQAHIDRE.
OrthoDBiEOG77M8QM.
PhylomeDBiP05771.
TreeFamiTF351133.

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.
IPR002290. Ser/Thr_dual-sp_kinase.
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. Align

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

Note: Contains a phosphoserine at position 660. Contains a phosphothreonine at position 641.

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691V → G in CAA44393. (PubMed:7880442)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441V → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042304
Natural varianti496 – 4961V → M in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_042305
Natural varianti588 – 5881P → H.1 Publication
Corresponds to variant rs35631544 [ dbSNP | Ensembl ].
VAR_042306

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei622 – 67150RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II. 2 PublicationsVSP_004738Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000498058; ENSP00000454428; ENSG00000166501.
GeneIDi5579.
KEGGihsa:5579.
UCSCiuc002dmd.3. human. [P05771-1]
uc002dme.3. human. [P05771-2]

Polymorphism databases

DMDMi20141488.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10618.1. [P05771-1 ]
CCDS10619.1. [P05771-2 ]
PIRi B24664. KIHUC2.
S00159. KIHUC1.
RefSeqi NP_002729.2. NM_002738.6. [P05771-2 ]
NP_997700.1. NM_212535.2. [P05771-1 ]
UniGenei Hs.460355.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I0E X-ray 2.60 A/B 321-671 [» ]
ProteinModelPortali P05771.
SMRi P05771. Positions 37-668.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111565. 57 interactions.
DIPi DIP-34187N.
IntActi P05771. 18 interactions.
MINTi MINT-240997.

Chemistry

BindingDBi P05771.
ChEMBLi CHEMBL2096620.
DrugBanki DB00675. Tamoxifen.
DB00163. Vitamin E.
GuidetoPHARMACOLOGYi 1483.

PTM databases

PhosphoSitei P05771.

Polymorphism databases

DMDMi 20141488.

Proteomic databases

MaxQBi P05771.
PaxDbi P05771.
PRIDEi P05771.

Protocols and materials databases

DNASUi 5579.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303531 ; ENSP00000305355 ; ENSG00000166501 . [P05771-2 ]
ENST00000321728 ; ENSP00000318315 ; ENSG00000166501 . [P05771-1 ]
ENST00000498058 ; ENSP00000454428 ; ENSG00000166501 .
GeneIDi 5579.
KEGGi hsa:5579.
UCSCi uc002dmd.3. human. [P05771-1 ]
uc002dme.3. human. [P05771-2 ]

Organism-specific databases

CTDi 5579.
GeneCardsi GC16P023847.
HGNCi HGNC:9395. PRKCB.
HPAi CAB003843.
MIMi 176970. gene.
neXtProti NX_P05771.
PharmGKBi PA33761.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118891.
HOVERGENi HBG108317.
InParanoidi P05771.
KOi K02677.
OMAi QAHIDRE.
OrthoDBi EOG77M8QM.
PhylomeDBi P05771.
TreeFami TF351133.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 2681.
Reactomei REACT_1178. Disinhibition of SNARE formation.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1280. Response to elevated platelet cytosolic Ca2+.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_19333. G alpha (z) signalling events.
REACT_200828. Depolymerisation of the Nuclear Lamina.
SignaLinki P05771.

Miscellaneous databases

ChiTaRSi PRKCB. human.
EvolutionaryTracei P05771.
GeneWikii PRKCB1.
GenomeRNAii 5579.
NextBioi 21632.
PMAP-CutDB P05771.
PROi P05771.
SOURCEi Search...

Gene expression databases

Bgeei P05771.
ExpressionAtlasi P05771. baseline and differential.
Genevestigatori P05771.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000961. 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.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000550. PKC_alpha. 1 hit.
PRINTSi PR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
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Publicationsi

« Hide 'large scale' publications
  1. "Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways."
    Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A.
    Science 233:859-866(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II).
  2. "Primary structures of human protein kinase C beta I and beta II differ only in their C-terminal sequences."
    Kubo K., Ohno S., Suzuki K.
    FEBS Lett. 223:138-142(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II).
  3. NIEHS SNPs program
    Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Hippocampus.
  7. "Autoregulation of cloned human protein kinase C beta and gamma gene promoters in U937 cells."
    Mahajna J., King P., Parker P., Haley J.
    DNA Cell Biol. 14:213-222(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
  8. "Positive and negative regulation of the transcription of the human protein kinase C beta gene."
    Niino Y.S., Ohno S., Suzuki K.
    J. Biol. Chem. 267:6158-6163(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
  9. "Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters."
    Obeid L.M., Blobe G.C., Karolak L.A., Hannun Y.A.
    J. Biol. Chem. 267:20804-20810(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
  10. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19, ACETYLATION AT ALA-2.
    Tissue: Platelet.
  11. "The genomic structure of the human protein kinase C beta gene (PRKCB)."
    Greenham J.A., Adams M.D., Doggett N.A., Mole S.E.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-176.
  12. "Alternative splicing increases the diversity of the human protein kinase C family."
    Coussens L., Rhee L., Parker P.J., Ullrich A.
    DNA 6:389-394(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-671.
    Tissue: Fetal brain.
  13. "Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta-I/beta-II."
    Kubo K., Ohno S., Suzuki K.
    Nucleic Acids Res. 15:7179-7180(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-671.
  14. "PKCbeta modulates antigen receptor signaling via regulation of Btk membrane localization."
    Kang S.W., Wahl M.I., Chu J., Kitaura J., Kawakami Y., Kato R.M., Tabuchi R., Tarakhovsky A., Kawakami T., Turck C.W., Witte O.N., Rawlings D.J.
    EMBO J. 20:5692-5702(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BTK.
  15. "The protein kinase Cbeta-selective inhibitor, enzastaurin (LY317615.HCl), suppresses signaling through the AKT pathway, induces apoptosis, and suppresses growth of human colon cancer and glioblastoma xenografts."
    Graff J.R., McNulty A.M., Hanna K.R., Konicek B.W., Lynch R.L., Bailey S.N., Banks C., Capen A., Goode R., Lewis J.E., Sams L., Huss K.L., Campbell R.M., Iversen P.W., Neubauer B.L., Brown T.J., Musib L., Geeganage S., Thornton D.
    Cancer Res. 65:7462-7469(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  16. "The phosphatase PHLPP controls the cellular levels of protein kinase C."
    Gao T., Brognard J., Newton A.C.
    J. Biol. Chem. 283:6300-6311(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHLPP1 AND PHLPP2.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  18. "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.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641 AND SER-660 (ISOFORM BETA-II), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: FUNCTION IN HISTONE H3 PHOSPHORYLATION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH KDM1A; PKN1 AND ANDR.
  21. "Protein kinase C beta (PKC beta): normal functions and diseases."
    Kawakami T., Kawakami Y., Kitaura J.
    J. Biochem. 132:677-682(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  22. "Endothelial dysfunction in diabetes mellitus: molecular mechanisms and clinical implications."
    Tabit C.E., Chung W.B., Hamburg N.M., Vita J.A.
    Rev. Endocr. Metab. Disord. 11:61-74(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Structure of the catalytic domain of human protein kinase C beta II complexed with a bisindolylmaleimide inhibitor."
    Grodsky N., Li Y., Bouzida D., Love R., Jensen J., Nodes B., Nonomiya J., Grant S.
    Biochemistry 45:13970-13981(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 321-660 IN COMPLEX WITH INHIBITOR, PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
  25. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-144; MET-496 AND HIS-588.

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: October 29, 2014
This is version 191 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

External Data

Dasty 3