Reviewed,
UniProtKB/Swiss-Prot P24033 (CDC2B_XENLA)
Last modified
June 16, 2009.
Version 73.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cell division control protein 2-B EC=2.7.11.22 EC=2.7.11.23 Alternative name(s): Cell division control protein 2 homolog 2 p34 protein kinase 2 | ||||
| Gene names |
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| Organism | Xenopus laevis (African clawed frog) | ||||
| Taxonomic identifier | 8355 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Protein attributes
| Sequence length | 302 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis. Component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II By similarity. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. |
| Enzyme regulation | Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it. Ref.1 |
| Subunit structure | Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with spdya. Ref.1 Ref.4 Ref.5 |
| Subcellular location | Nucleus By similarity. |
| Sequence similarities | Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division Mitosis |
| Cellular component | Nucleus |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosisInferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylationInferred from electronic annotation. Source: InterPro |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase subunit kinase activityInferred from electronic annotation. Source: EC cyclin-dependent protein kinase activityInferred from electronic annotation. Source: EC protein binding Ref.4 Ref.5Inferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 302 | 302 | Cell division control protein 2-B | PRO_0000085736 | |||||
Regions | |||||||||
| Domain | 4 – 287 | 284 | Protein kinase | ||||||
| Nucleotide binding | 10 – 18 | 9 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 128 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 33 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 14 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 15 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 161 | 1 | Phosphothreonine; by CAK Ref.3 | ||||||
| Modified residue | 277 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 87 | 1 | L → V in AAA63562. Ref.1 | ||||||
| Sequence conflict | 123 | 1 | R → G in AAA63562. Ref.1 | ||||||
| Sequence conflict | 172 | 1 | S → P in AAA63562. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Requirement of mosXe protein kinase for meiotic maturation of Xenopus oocytes induced by a cdc2 mutant lacking regulatory phosphorylation sites." Pickham K.M., Meyer A.N., Li J., Donoghue D.J. Mol. Cell. Biol. 12:3192-3203(1992) [PubMed: 1377775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, SUBUNIT. Tissue: Oocyte. |
| [2] | NIH - Xenopus Gene Collection (XGC) project Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tadpole. |
| [3] | "The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues." Fesquet D., Labbe J.-C., Derancourt J., Capony J.-P., Galas S., Girard F., Lorca T., Shuttleworth J., Doree M., Cavadore J.-C. EMBO J. 12:3111-3121(1993) [PubMed: 8344251] [Abstract] Cited for: PHOSPHORYLATION AT THR-161. |
| [4] | "A novel p34cdc2 binding and activating protein that is necessary and sufficient to trigger G2/M progression in Xenopus oocytes." Ferby I., Blazquez M., Palmer A., Eritja R., Nebreda A.R. Genes Dev. 13:2177-2189(1999) [PubMed: 10465793] [Abstract] Cited for: INTERACTION WITH SPDYA. |
| [5] | "Identification and comparative analysis of multiple mammalian Speedy/Ringo proteins." Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J. Cell Cycle 4:155-165(2005) [PubMed: 15611625] [Abstract] Cited for: INTERACTION WITH SPDYA. |
Cross-references
Sequence databases | |
|---|---|
| M60681 mRNA. Translation: AAA63562.1. BC054146 mRNA. Translation: AAH54146.1. | |
| PIR | B44349. |
| RefSeq | NP_001080093.1. |
| UniGene | Xl.3815 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1P2A based on UniProtKB P24941. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 379785. |
| KEGG | xla:379785. |
Phylogenomic databases | |
| HOVERGEN | P24033. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.22. 648. 2.7.11.23. 648. |
Family and domain databases | |
| InterPro | IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view] |
| Pfam | PF00069. Pkinase. 1 hit. [Graphical view] |
| ProDom | PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00220. S_TKc. 1 hit. [Graphical view] |
| 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 | CDC2B_XENLA | ||||||||
| Accession | Primary (citable) accession number: P24033 Secondary accession number(s): Q7SZ44 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Xenopus annotation project | ||||||||

Clusters with


