Reviewed,
UniProtKB/Swiss-Prot Q05655 (KPCD_HUMAN)
Last modified
November 25, 2008.
Version 97.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein kinase C delta type EC=2.7.11.13 Alternative name(s): nPKC-delta | ||
| Gene names |
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| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 676 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in antigen-dependent control of B-cell function. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Enzyme regulation | Three specific sites; Thr-507 (activation loop of the kinase domain), Ser-645 (turn motif) and Ser-664 (hydrophobic region), need to be phosphorylated for its full activation. |
| Subunit structure | Interacts with PDK1, RAD9A, CDCP1 and MUC1. |
| Subcellular location | CytoplasmBy similarity. Membrane; Peripheral membrane proteinBy similarity. |
| Domain | The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor. The C2 domain is a non-calcium binding domain. It binds proteins containing phosphotyrosine in a sequence-specific manner. |
| Post-translational modification | Phosphorylated on Thr-507, within the activation loop. Autophosphorylated and/or phosphorylated. Although the Thr-507 phosphorylation occurs it is not a prerequisite for enzymatic activity By similarity. |
| 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
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| FYN | P06241 | 3 | EBI-704279,EBI-515315 | |
| GAP43 | P17677 | 3 | EBI-704279,EBI-1267511 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 676 | 676 | Protein kinase C delta type | PRO_0000055694 | |||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||
| Domain | 1 – 90 | 90 | C2 | ||||||||||||||||||||||||
| Domain | 349 – 603 | 255 | Protein kinase | ||||||||||||||||||||||||
| Domain | 604 – 675 | 72 | AGC-kinase C-terminal | ||||||||||||||||||||||||
| Zinc finger | 158 – 208 | 51 | Phorbol-ester/DAG-type 1 | ||||||||||||||||||||||||
| Zinc finger | 230 – 280 | 51 | Phorbol-ester/DAG-type 2 | ||||||||||||||||||||||||
| Nucleotide binding | 355 – 363 | 9 | ATP By similarity | ||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||
| Active site | 473 | 1 | Proton acceptor By similarity | ||||||||||||||||||||||||
| Binding site | 378 | 1 | ATP By similarity | ||||||||||||||||||||||||
| Site | 48 | 1 | Interaction with phosphotyrosine-containing peptide | ||||||||||||||||||||||||
| Site | 62 | 1 | Interaction with phosphotyrosine-containing peptide | ||||||||||||||||||||||||
| Site | 67 | 1 | Interaction with phosphotyrosine-containing peptide | ||||||||||||||||||||||||
| Site | 123 | 1 | Interaction with phosphotyrosine-containing peptide | ||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||
| Modified residue | 130 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 302 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 304 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 307 | 1 | Phosphoserine | ||||||||||||||||||||||||
| Modified residue | 313 | 1 | Phosphotyrosine | ||||||||||||||||||||||||
| Modified residue | 334 | 1 | Phosphotyrosine | ||||||||||||||||||||||||
| Modified residue | 374 | 1 | Phosphotyrosine | ||||||||||||||||||||||||
| Modified residue | 507 | 1 | Phosphothreonine; by PDPK1 By similarity | ||||||||||||||||||||||||
| Modified residue | 645 | 1 | Phosphoserine Potential | ||||||||||||||||||||||||
| Modified residue | 664 | 1 | Phosphoserine | ||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||
| Natural variant | 348 | 1 | N → S: dbSNP rs33911937. | VAR_035347 | |||||||||||||||||||||||
| Natural variant | 375 | 1 | F → S: dbSNP rs1056998. | VAR_006175 | |||||||||||||||||||||||
| Natural variant | 410 | 1 | L → F: dbSNP rs34502209. | VAR_035348 | |||||||||||||||||||||||
| Natural variant | 483 | 1 | R → W: dbSNP rs35891605. | VAR_046009 | |||||||||||||||||||||||
| Natural variant | 494 | 1 | M → V | VAR_020610 | |||||||||||||||||||||||
| Natural variant | 593 | 1 | V → M | VAR_006176 | |||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||
| Sequence conflict | 524 | 1 | K → R in BAG36031. Ref.2 | ||||||||||||||||||||||||
| Sequence conflict | 533 | 1 | S → A Ref.7 | ||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Beta strand | 1 – 13 | 13 | |||||||||||||||||||||||||
| Beta strand | 20 – 23 | 4 | |||||||||||||||||||||||||
| Beta strand | 27 – 38 | 12 | |||||||||||||||||||||||||
| Beta strand | 41 – 45 | 5 | |||||||||||||||||||||||||
| Beta strand | 58 – 62 | 5 | |||||||||||||||||||||||||
| Beta strand | 68 – 76 | 9 | |||||||||||||||||||||||||
| Beta strand | 79 – 87 | 9 | |||||||||||||||||||||||||
| Helix | 88 – 96 | 9 | |||||||||||||||||||||||||
| Turn | 97 – 100 | 4 | |||||||||||||||||||||||||
| Beta strand | 101 – 107 | 7 | |||||||||||||||||||||||||
| Beta strand | 109 – 111 | 3 | |||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular and biochemical characterization of a recombinant human PKC-delta family member." Aris J.P., Basta P.V., Holmes W.D., Ballas L.M., Moomaw C., Rankl N.B., Blobel G., Loomis C.R., Burns D.J. Biochim. Biophys. Acta 1174:171-181(1993) [PubMed: 8357834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-375 AND MET-593. Tissue: Liver. |
| [2] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin. |
| [5] | "Partial cDNA Sequence of human protein kinase C delta." Hug H. Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-365. Tissue: Hippocampus. |
| [6] | "Functional analyses of mammalian protein kinase C isozymes in budding yeast and mammalian fibroblasts." Nomoto S., Watanabe Y., Ninomiya-Tsuji J., Yang L.-X., Kikuchi K., Hagiwara M., Hidaka H., Matsumoto K., Irie K. Genes Cells 2:601-614(1997) [PubMed: 9427282] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-676. |
| [7] | "Identification of multiple, novel, protein kinase C-related gene products." Palmer R.H., Ridden J., Parker P.J. FEBS Lett. 356:5-8(1994) [PubMed: 7988719] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-533, VARIANT VAL-494. |
| [8] | "Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling." Ren J., Li Y., Kufe D. J. Biol. Chem. 277:17616-17622(2002) [PubMed: 11877440] [Abstract] Cited for: INTERACTION WITH MUC1, FUNCTION. |
| [9] | "Protein kinase Cdelta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9." Yoshida K., Wang H.-G., Miki Y., Kufe D. EMBO J. 22:1431-1441(2003) [PubMed: 12628935] [Abstract] Cited for: INTERACTION WITH RAD9A. |
| [10] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, MASS SPECTROMETRY. Tissue: Epithelium. |
| [11] | "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-313; TYR-334 AND TYR-374, MASS SPECTROMETRY. |
| [12] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, MASS SPECTROMETRY. Tissue: Platelet. |
| [13] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-302; SER-304; SER-307 AND SER-664, MASS SPECTROMETRY. |
| [14] | "The C2 domain of PKCdelta is a phosphotyrosine binding domain." Benes C.H., Wu N., Elia A.E.H., Dharia T., Cantley L.C., Soltoff S.P. Cell 121:271-280(2005) [PubMed: 15851033] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-123 IN COMPLEX WITH PHOSPHOTYROSINE-CONTAINING PEPTIDE, INTERACTION WITH CDCP1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | ||||||||
|---|---|---|---|---|---|---|---|---|
| L07860 mRNA. Translation: AAA03176.1. L07861 mRNA. Translation: AAA03175.1. AK313216 mRNA. Translation: BAG36031.1. CH471055 Genomic DNA. Translation: EAW65279.1. BC043350 mRNA. Translation: AAH43350.1. Z22521 mRNA. Translation: CAA80249.1. D10495 mRNA. Translation: BAA01381.1. | ||||||||
| PIR | S35704. | |||||||
| RefSeq | NP_006245.2. NP_997704.1. | |||||||
| UniGene | Hs.155342 | |||||||
3D structure databases | ||||||||
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Clusters with