Reviewed,
UniProtKB/Swiss-Prot Q8BZ03 (KPCD2_MOUSE)
Last modified
February 9, 2010.
Version 72.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Serine/threonine-protein kinase D2 EC=2.7.11.13 Alternative name(s): nPKC-D2 | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 875 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress By similarity. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Cofactor | Magnesium By similarity. |
| Enzyme regulation | Activated by DAG and phorbol esters. Phorbol-ester/DAG-type domains bind DAG, mediating translocation to membranes. Autophosphorylation of Ser-711 and phosphorylation of Ser-707 by PKC relieves auto-inhibition by the PH domain By similarity. |
| Subcellular location | Cytoplasm By similarity. Membrane By similarity. Note: Translocation to the cell membrane is required for kinase activation By similarity. |
| Post-translational modification | Phosphorylation of Ser-873 correlates with the activation status of the kinase By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily. Contains 1 PH domain. Contains 2 phorbol-ester/DAG-type zinc fingers. Contains 1 protein kinase domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Membrane |
| Domain | Repeat Zinc-finger |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | intracellular signaling cascade Inferred from electronic annotation. Source: InterPro protein amino acid phosphorylationInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein kinase C activityInferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 875 | 875 | Serine/threonine-protein kinase D2 | PRO_0000260436 | |||||
Regions | |||||||||
| Domain | 398 – 510 | 113 | PH | ||||||
| Domain | 552 – 808 | 257 | Protein kinase | ||||||
| Zinc finger | 138 – 188 | 51 | Phorbol-ester/DAG-type 1 | ||||||
| Zinc finger | 265 – 315 | 51 | Phorbol-ester/DAG-type 2 | ||||||
| Nucleotide binding | 558 – 566 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 675 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 581 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 189 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 197 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 198 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 199 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 200 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 203 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 206 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 211 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 212 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 214 | 1 | Phosphoserine Ref.3 | ||||||
| Modified residue | 225 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 227 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 236 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 237 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 238 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 339 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 354 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 356 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 363 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 375 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 376 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 397 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 519 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 707 | 1 | Phosphoserine; by PKC By similarity | ||||||
| Modified residue | 711 | 1 | Phosphoserine; by autocatalysis By similarity | ||||||
| Modified residue | 718 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 873 | 1 | Phosphoserine; by autocatalysis By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 213 | 1 | E → G in BAE42012. Ref.1 | ||||||
| Sequence conflict | 220 | 1 | E → G in BAE41652. Ref.1 | ||||||
| Sequence conflict | 310 | 1 | R → H in BAE32326. Ref.1 | ||||||
| Sequence conflict | 310 | 1 | R → H in BAE41652. Ref.1 | ||||||
| Sequence conflict | 630 | 1 | K → N in BAE42012. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Thymus and Vagina. |
| [2] | "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]. Strain: FVB/N. Tissue: Colon and Mammary tumor. |
| [3] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-211; SER-212 AND SER-214, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK037030 mRNA. Translation: BAC29677.1. AK154029 mRNA. Translation: BAE32326.1. AK170236 mRNA. Translation: BAE41652.1. AK170761 mRNA. Translation: BAE42012.1. BC095949 mRNA. Translation: AAH95949.1. BC096444 mRNA. Translation: AAH96444.1. |
| IPI | IPI00227209. |
| RefSeq | NP_849231.1. |
| UniGene | Mm.1881 |
3D structure databases | |
| HSSP | HSSP built from PDB template 2COA based on UniProtKB Q9BZL6. |
| SMR | Q8BZ03. Positions 130-192, 263-315, 396-510, 542-812. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q8BZ03. |
Proteomic databases | |
| PRIDE | Q8BZ03. |
Genome annotation databases | |
| Ensembl | ENSMUST00000086104; ENSMUSP00000083273; ENSMUSG00000041187; Mus musculus. [Genome view] |
| GeneID | 101540. |
| KEGG | mmu:101540. |
| UCSC | uc009fig.1. mouse. |
Organism-specific databases | |
| CTD | 101540. |
| MGI | MGI:2141917. Prkd2. |
Phylogenomic databases | |
| eggNOG | roNOG09017. |
| HOGENOM | HBG314865. |
| HOVERGEN | Q8BZ03. |
| InParanoid | Q8BZ03. |
| OMA | ASPWSHI. |
| OrthoDB | EOG9FXTT2. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.13. 244. |
Gene expression databases | |
| ArrayExpress | Q8BZ03. |
| Bgee | Q8BZ03. |
| CleanEx | MM_PRKD2. |
| Genevestigator | Q8BZ03. |
| GermOnline | ENSMUSG00000041187. Mus musculus. |
Family and domain databases | |
| InterPro | IPR020454. DAG/PE_bd. IPR011009. Kinase-like_dom. IPR011993. PH_type. IPR001849. Pleckstrin_homology. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR015727. Protein_Kinase_C_mu-related. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view] |
| Gene3D | G3DSA:2.30.29.30. PH_type. 1 hit. |
| PANTHER | PTHR22968. PKC_mu_like. 1 hit. |
| Pfam | PF00130. C1_1. 2 hits. PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view] |
| PRINTS | PR00008. DAGPEDOMAIN. |
| SMART | SM00109. C1. 2 hits. SM00233. PH. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view] |
| PROSITE | PS50003. PH_DOMAIN. 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 Resources | |
| NextBio | 355000. |
| SOURCE | Search... |
Entry information
| Entry name | KPCD2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8BZ03 Secondary accession number(s): Q3TCE5, Q3TDF0, Q3U4V4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| Human and mouse protein kinases Human and mouse protein kinases: classification and index |
| SIMILARITY comments Index of protein domains and families |

Clusters with


