P68403 (KPCB_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	671 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 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. Ref.10 Ref.11
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Binds 3 calcium ions per subunit. The ions are bound to the C2 domain.
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.
Subcellular location	Cytoplasm. Nucleus By similarity. Membrane; Peripheral membrane protein.
Post-translational modification	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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.13
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 process	Adaptive immunity Apoptosis Immunity Transcription Transcription regulation
Cellular component	Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding Zinc
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Uncategorized	regulation of transcription from RNA polymerase II promoter by nuclear hormone receptor Inferred from sequence or structural similarity. Source: UniProtKB
Biological process	B cell activation Inferred from sequence or structural similarity. Source: UniProtKB B cell receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signal transduction Non-traceable author statement. Source: RGD positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of odontogenesis of dentin-containing tooth Inferred from expression pattern. Source: RGD regulation of dopamine secretion Inferred from mutant phenotype. Source: RGD regulation of growth Inferred from mutant phenotype Ref.3. Source: RGD response to drug Inferred from mutant phenotype. Source: RGD response to ethanol Inferred from expression pattern. Source: RGD response to glucose stimulus Inferred from expression pattern. Source: RGD response to vitamin D Inferred from expression pattern. Source: RGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	brush border membrane Inferred from direct assay. Source: RGD centrosome Inferred from direct assay. Source: RGD cytosol Inferred from direct assay. Source: RGD membrane fraction Inferred from direct assay. Source: RGD nucleus Inferred from sequence or structural similarity. Source: UniProtKB soluble fraction Inferred from direct assay. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW androgen receptor binding Inferred from sequence or structural similarity. Source: UniProtKB 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 binding Inferred from physical interaction. Source: IntAct protein kinase C activity Inferred from direct assay. Source: RGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRIM41	Q8WV44-2	3	EBI-397092,EBI-726015	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Beta-I (identifier: P68403-1)

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: P68403-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 671

670

Protein kinase C beta type

PRO_0000055687

Regions

Domain

173 – 260

88

C2

Domain

342 – 600

259

Protein kinase

Domain

601 – 671

71

AGC-kinase C-terminal

Zinc finger

36 – 86

51

Phorbol-ester/DAG-type 1

Zinc finger

101 – 151

51

Phorbol-ester/DAG-type 2

Nucleotide binding

348 – 356

9

ATP By similarity

Sites

Active site

466

1

Proton acceptor By similarity

Metal binding

186

1

Calcium 1; via carbonyl oxygen

Metal binding

187

1

Calcium 1

Metal binding

187

1

Calcium 2

Metal binding

193

1

Calcium 2

Metal binding

246

1

Calcium 1

Metal binding

246

1

Calcium 2

Metal binding

247

1

Calcium 2; via carbonyl oxygen

Metal binding

248

1

Calcium 1

Metal binding

248

1

Calcium 2

Metal binding

248

1

Calcium 3

Metal binding

251

1

Calcium 3

Metal binding

252

1

Calcium 3; via carbonyl oxygen

Metal binding

254

1

Calcium 1

Metal binding

254

1

Calcium 3

Binding site

371

1

ATP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

16

1

Phosphoserine; by autocatalysis Ref.7

Modified residue

17

1

Phosphothreonine; by autocatalysis Ref.7

Modified residue

195

1

Phosphotyrosine By similarity

Modified residue

250

1

Phosphothreonine; by autocatalysis By similarity

Modified residue

314

1

Phosphothreonine; by autocatalysis Ref.7

Modified residue

324

1

Phosphothreonine; by autocatalysis Ref.7

Modified residue

500

1

Phosphothreonine; by PDPK1 Probable

Modified residue

504

1

Phosphothreonine By similarity

Modified residue

635

1

Phosphothreonine; by autocatalysis Ref.7

Modified residue

642

1

Phosphothreonine; by autocatalysis Ref.6 Ref.7 Ref.8 Ref.13

Modified residue

661

1

Phosphoserine; by autocatalysis Ref.6 Ref.13

Modified residue

662

1

Phosphotyrosine; by SYK By similarity

Natural variations

Alternative sequence

622 – 671

50

RDKRD…FVINV → CGRNAENFDRFFTRHPPVLT PPDQEVIRNIDQSEFEGFSF VNSEFLKPEVKS in isoform Beta-II.

VSP_004739

Experimental info

Mutagenesis

16 – 17

2

ST → AA: No effect.

Mutagenesis

314

1

T → A: No effect; when associated with A-323. Ref.7

Mutagenesis

324

1

T → A: No effect; when associated with A-313. Ref.7

Mutagenesis

500

1

T → E: 50% increase of enzymatic activity. Ref.9

Mutagenesis

500

1

T → S: 50% decrease of enzymatic activity. Ref.9

Mutagenesis

500

1

T → V or D: Loss of enzymatic activity. Ref.9

Mutagenesis

635

1

T → 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. Ref.7 Ref.8

Mutagenesis

642

1

T → 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. Ref.7 Ref.8

Sequence conflict

25

1

A → P in AAA41868. Ref.3

Sequence conflict

126

1

I → V in AAA41875. Ref.1

Sequence conflict

138

1

N → S in AAA41875. Ref.1

Sequence conflict

141

1

K → R in AAA41875. Ref.1

Sequence conflict

149

1

S → G in AAA41875. Ref.1

Sequence conflict

164

1

I → V in AAA41875. Ref.1

Sequence conflict

170 – 171

2

RE → GG in AAA41875. Ref.1

Sequence conflict

174

1

I → V in AAA41875. Ref.1

Sequence conflict

294

1

G → E in AAA41868. Ref.3

Sequence conflict

419

1

V → M in CAA28035. Ref.2

Sequence conflict

419

1

V → M in CAA28036. Ref.2

Sequence conflict

628

1

Missing in AAA41865. Ref.1

Sequence conflict

640

1

Missing in AAA41865. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

671

Helix Strand Turn

Details...

Beta strand

161 – 182

22

Beta strand

194 – 202

9

Beta strand

222 – 230

9

Helix

234 – 237

4

Beta strand

239 – 246

8

Beta strand

249 – 251

3

Beta strand

254 – 262

9

Helix

263 – 266

4

Beta strand

271 – 276

6

Helix

280 – 283

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta-I [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A1935030F758513C	FASTA	671	76,751
	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
	Isoform Beta-II [UniParc] [UniParc]. Checksum: A65573AAF6E224C7	FASTA	673	76,894
	10 20 30 40 50 60 MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF 70 80 90 100 110 120 GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS 130 140 150 160 170 180 LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR EVLIVVVRDA 190 200 210 220 230 240 KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL 250 260 270 280 290 300 SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE 310 320 330 340 350 360 LRQKFERAKI GQGTKAPEEK TANTISKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE 370 380 390 400 410 420 RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM 430 440 450 460 470 480 EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI 490 500 510 520 530 540 KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP 550 560 570 580 590 600 FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF 610 620 630 640 650 660 RYIDWEKLER KEIQPPYKPK ACGRNAENFD RFFTRHPPVL TPPDQEVIRN IDQSEFEGFS 670 FVNSEFLKPE VKS

References

[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: 3755379] [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: 2428667] [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: 3345563] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-I). Tissue: Fibroblast.
[4]	"Cloning of rat brain protein kinase C complementary DNA." Ono Y., Kurokawa T., Kawahara K., Nishimura O., Marumoto R., Igarashi K., Sugino Y., Kikkawa U., Ogita K., Nishizuka Y. FEBS Lett. 203:111-115(1986) [PubMed: 3755404] [Abstract] 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: 3469647] [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: 8749392] [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: 8327493] [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: 8034726] [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: 7961692] [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: 10938109] [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: 11714718] [Abstract] Cited for: FUNCTION IN INSULIN SIGNALING.
[12]	"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: 9817842] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 157-288 IN COMPLEX WITH CALCIUM IONS.
[13]	"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: 21215369] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 1-661 IN COMPLEX WITH CALCIUM IONS, PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00189278.
IPI00230864.

PIR

KIRTC1. A00622.

RefSeq

NP_001165776.1. NM_001172305.1.
NP_036845.3. NM_012713.3.

UniGene

Rn.91118.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A25	X-ray	2.70	A/B	157-289	[»]
3PFQ	X-ray	4.00	A	1-661	[»]

ProteinModelPortal

P68403.

SMR

P68403. Positions 37-668.

ModBase

Search...

Protein-protein interaction databases

IntAct

P68403. 3 interactions.

STRING

P68403.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

25023.

KEGG

rno:25023.

Organism-specific databases

CTD

5579.

RGD

3396. Prkcb.

Phylogenomic databases

eggNOG

maNOG17521.

GeneTree

ENSGT00590000082854.

HOVERGEN

HBG108317.

PhylomeDB

P68403.

Gene expression databases

ArrayExpress

P68403.

Genevestigator

P68403.

GermOnline

ENSRNOG00000012061. Rattus norvegicus.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR020477. C2_dom.
IPR018029. C2_membr_targeting.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
[Graphical view]

KO

K02677.

Pfam

PF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000550. PKC_alpha. 1 hit.

PRINTS

PR00360. C2DOMAIN.
PR00008. DAGPEDOMAIN.

SMART

SM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

605147.

Entry information

Entry name

KPCB_RAT

Accession

Primary (citable) accession number: P68403
Secondary accession number(s): P04410, P04411

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program