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UniProtKB/Swiss-Prot entry P28867


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KPCD_MOUSE
Primary accession number P28867
Secondary accession numbers Q91V85 Q9Z333
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on March 27, 2002 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 94)
Name and origin of the protein
Protein name Protein kinase C delta type
Synonyms EC 2.7.11.13
nPKC-delta
Gene name
Name: Prkcd
Synonyms: Pkcd
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1021/bi00246a008; PubMed=1868068 [NCBI, ExPASy, EBI, Israel, Japan]
Mischak H., Bodenteich A., Kolch W., Goodnight J., Hofer F., Mushinski J.F.;
"Mouse protein kinase C-delta, the major isoform expressed in mouse hemopoietic cells: sequence of the cDNA, expression patterns, and characterization of the protein.";
Biochemistry 30:7925-7931(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=ICR;
TISSUE=Brain;
PubMed=1765103 [NCBI, ExPASy, EBI, Israel, Japan]
Mizuno K., Kubo K., Saido T.C., Akita Y., Osada S., Kuroki T., Ohno S., Suzuki K.;
"Structure and properties of a ubiquitously expressed protein kinase C, nPKC delta.";
Eur. J. Biochem. 202:931-940(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
STRAIN=129/SvJ;
Wheeler D.L., Gillis M.E., Verma A.K.;
"Intron/exon structure of the murine protein kinase C delta gene.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1248/bpb.24.973; PubMed=11558579 [NCBI, ExPASy, EBI, Israel, Japan]
Sakurai Y., Onishi Y., Tanimoto Y., Kizaki H.;
"Novel protein kinase C delta isoform insensitive to caspase-3.";
Biol. Pharm. Bull. 24:973-977(2001).
[5]
FUNCTION.
DOI=10.1038/416860a; PubMed=11976686 [NCBI, ExPASy, EBI, Israel, Japan]
Mecklenbraeuker I., Saijo K., Zheng N.Y., Leitges M., Tarakhovsky A.;
"Protein kinase Cdelta controls self-antigen-induced B-cell tolerance.";
Nature 416:860-865(2002).
[6]
PHOSPHORYLATION AT THR-505.
DOI=10.1126/science.281.5385.2042; PubMed=9748166 [NCBI, ExPASy, EBI, Israel, Japan]
Le Good J.A., Ziegler W.H., Parekh D.B., Alessi D.R., Cohen P., Parker P.J.;
"Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1.";
Science 281:2042-2045(1998).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND MASS SPECTROMETRY.
TISSUE=Mast cell;
PubMed=17947660 [NCBI, ExPASy, EBI, Israel, Japan]
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling.";
J. Immunol. 179:5864-5876(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[9]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 231-280 IN COMPLEX WITH PHORBOL ESTER AND ZINC IONS.
DOI=10.1016/0092-8674(95)90011-X; PubMed=7781068 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang G., Kazanietz M.G., Blumberg P.M., Hurley J.H.;
"Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester.";
Cell 81:917-924(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M69042; AAA73056.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60304; CAA42845.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF274044; AAF79208.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF251036; AAF64316.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB011812; BAA36408.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40281; KIMSCD.
RefSeq NP_035233.1; -.
UniGene Mm.2314
3D structure databases
PDB
1PTQ; X-ray; 1.95 A; A=231-280.[ExPASy / RCSB / EBI]
1PTR; X-ray; 2.20 A; A=231-280.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1PTQ; -.
1PTR; -.
SMR P28867; 1-123, 344-616.
ModBase P28867.
Protein-protein interaction databases
DIP DIP:1169N; -.
IntAct P28867; -.
PTM databases
PhosphoSite P28867; -.
Organism-specific databases
MGI MGI:97598; Prkcd.
Gene expression databases
ArrayExpress P28867; -.
CleanEx MM_PRKCD; -.
GermOnline ENSMUSG00000021948; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0019992; Molecular function: diacylglycerol binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004697; Molecular function: protein kinase C activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042100; Biological process: B cell proliferation (inferred from mutant phenotype from MGI).
GO:0016064; Biological process: immunoglobulin mediated immune response (inferred from mutant phenotype from MGI).
GO:0032613; Biological process: interleukin-10 production (inferred from mutant phenotype from MGI).
GO:0032615; Biological process: interleukin-12 production (inferred from mutant phenotype from MGI).
GO:0007242; Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000008; C2_Ca-dep.
IPR002219; DAG_PE_bd.
IPR015745; PKC.
IPR000961; Pkinase_C.
IPR014376; Prot_kin_PKC_delta.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
PANTHER PTHR22985:SF86; PKC; 1.
Pfam PF00130; C1_1; 2.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000551; PKC_delta; 1.
PRINTS PR00008; DAGPEDOMAIN.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00109; C1; 2.
SM00239; C2; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS50004; C2; FALSE_NEG.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P28867.
ProtoNet P28867.
Genome annotation databases
Ensembl ENSMUSG00000021948; Mus musculus. [Contig view]
GeneID 18753; -.
KEGG mmu:18753; -.
Phylogenomic databases
HOGENOM P28867; -.
HOVERGEN P28867; -.
Other
LinkHub P28867; -.
NextBio 294929; -.
SOURCE Prkcd; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane; Metal-binding; Nucleotide-binding; Phorbol-ester binding; Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   674  674     Protein kinase C delta type. PRO_0000055695
DOMAIN   1    90  90     C2. 
DOMAIN   347   601  255     Protein kinase. 
DOMAIN   602   673  72     AGC-kinase C-terminal. 
ZN_FING   158   208  51     Phorbol-ester/DAG-type 1. 
ZN_FING   230   280  51     Phorbol-ester/DAG-type 2. 
NP_BIND   353   361  9     ATP (By similarity). 
ACT_SITE   471   471        Proton acceptor (By similarity). 
BINDING   376   376        ATP (By similarity). 
SITE   48    48  1     Interaction with phosphotyrosine-containing peptide (By similarity). 
SITE   62    62  1     Interaction with phosphotyrosine-containing peptide (By similarity). 
SITE   67    67  1     Interaction with phosphotyrosine-containing peptide (By similarity). 
SITE   123   123  1     Interaction with phosphotyrosine-containing peptide (By similarity). 
MOD_RES   130   130        Phosphoserine (By similarity). 
MOD_RES   311   311        Phosphotyrosine. 
MOD_RES   332   332        Phosphotyrosine (By similarity). 
MOD_RES   372   372        Phosphotyrosine (By similarity). 
MOD_RES   505   505        Phosphothreonine; by PDPK1 (By similarity). 
MOD_RES   643   643        Phosphoserine (Probable). 
MOD_RES   662   662        Phosphoserine (By similarity). 
VAR_SEQ   326   326        L -> LGEAGSHISLKLSFPSRAKEKDSSETC (in isoform 2). VSP_004741
CONFLICT   214   214        N -> I (in Ref. 4; BAA36408). 
CONFLICT   226   226        N -> S (in Ref. 4; BAA36408). 
CONFLICT   319   319        E -> D (in Ref. 1; AAA73056). 
CONFLICT   330   330        G -> W (in Ref. 1; AAA73056). 
CONFLICT   337   337        E -> V (in Ref. 1; AAA73056). 
CONFLICT   501   501        G -> D (in Ref. 1; AAA73056). 
CONFLICT   503   503        A -> P (in Ref. 1; AAA73056). 
CONFLICT   513   513        I -> S (in Ref. 1; AAA73056). 
CONFLICT   518   520        LQG -> PARA (in Ref. 4; BAA36408). 
CONFLICT   538   538        E -> R (in Ref. 4; BAA36408). 
STRAND   233   236  4      
TURN   245   247  3      
STRAND   253   256  4      
STRAND   258   261  4      
TURN   262   264  3      
HELIX   270   275  6      
Sequence information
Length: 674 AA [This is the length of the unprocessed precursor] Molecular weight: 77547 Da [This is the MW of the unprocessed precursor] CRC64: 6E9F753348F03D59 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPFLRISFN SYELGSLQVE DEASQPFCAV KMKEALSTER GKTLVQKKPT MYPEWKTTFD 

        70         80         90        100        110        120 
AHIYEGRVIQ IVLMRAAEDP VSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMCVQY 

       130        140        150        160        170        180 
FLEDGDCKQS MRSEEEAKFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKEFVW 

       190        200        210        220        230        240 
GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS 

       250        260        270        280        290        300 
PTFCDHCGSL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRSSR 

       310        320        330        340        350        360 
KLDTTESVGI YQGFEKKPEV SGSDILDNNG TYGKIWEGST RCTLENFTFQ KVLGKGSFGK 

       370        380        390        400        410        420 
VLLAELKGKD KYFAIKCLKK DVVLIDDDVE CTMVEKRVLA LAWESPFLTH LICTFQTKDH 

       430        440        450        460        470        480 
LFFVMEFLNG GDLMFHIQDK GRFELYRATF YAAEIICGLQ FLHSKGIIYR DLKLDNVMLD 

       490        500        510        520        530        540 
RDGHIKIADF GMCKENIFGE GRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML 

       550        560        570        580        590        600 
IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPDKRLG VTGNIRIHPF 

       610        620        630        640        650        660 
FKTINWSLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI DSMDQEAFHG 

       670 
FSFVNPKFEQ FLDI 

P28867 in FASTA format

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