Reviewed,
UniProtKB/Swiss-Prot A2CI34 (DUSTY_PIMPR)
Last modified
October 13, 2009.
Version 20.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dual serine/threonine and tyrosine protein kinase EC=2.7.12.1 Alternative name(s): Dusty protein kinase Short name=Dusty PK Receptor-interacting serine/threonine-protein kinase 5 | ||||
| Gene names |
| ||||
| Organism | Pimephales promelas (Fathead minnow) | ||||
| Taxonomic identifier | 90988 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Pimephales |
Protein attributes
| Sequence length | 903 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | May induce both caspase-dependent apoptosis and caspase-independent cell death By similarity. UniProtKB Q6XUX3 |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. UniProtKB P16879 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Coiled coil |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase |
| Gene Ontology (GO) | |
| Biological process | protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activityInferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activityInferred 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 – 903 | 903 | Dual serine/threonine and tyrosine protein kinase | PRO_0000374057 | |||||
Regions | |||||||||
| Domain | 627 – 881 | 255 | Protein kinase | ||||||
| Nucleotide binding | 633 – 641 | 9 | ATP By similarity | ||||||
| Coiled coil | 382 – 414 | 33 | Potential | ||||||
Sites | |||||||||
| Active site | 752 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 656 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Dusty protein kinases: primary structure, gene evolution, tissue specific expression and unique features of the catalytic domain." Peng J., Dong W., Chen Y., Mo R., Cheng J.-F., Hui C.-C., Mohandas N., Huang C.-H. Biochim. Biophys. Acta 1759:562-572(2006) [PubMed: 17123648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| DQ419945 mRNA. Translation: ABD77593.1. | |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | A2CI34. |
Family and domain databases | |
| InterPro | IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view] |
| Pfam | PF00069. Pkinase. 1 hit. [Graphical view] |
| ProDom | PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DUSTY_PIMPR | ||||||||
| Accession | Primary (citable) accession number: A2CI34 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

Clusters with


