Reviewed,
UniProtKB/Swiss-Prot O55076 (CDK2_CRIGR)
Last modified
October 13, 2009.
Version 71.
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 protein kinase 2 EC=2.7.11.22 | ||
| Gene names |
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| Organism | Cricetulus griseus (Chinese hamster) | ||
| Taxonomic identifier | 10029 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus |
Protein attributes
| Sequence length | 298 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Involved in the control of the cell cycle. Interacts with cyclins A, B1, B3, D, or E. Activity of CDK2 is maximal during S phase and G2 By similarity. |
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Enzyme regulation | Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-160 activates it By similarity. |
| Subunit structure | Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts with CABLES1. Interacts with UHRF2. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo proteins SPDYA and SPDYC. Found in a complex with both SPDYA and CDKN1B/KIP1 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 |
| Coding sequence diversity | Alternative splicing |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Acetylation 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 |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Select] | ||||||
| Isoform CDK2-alpha (identifier: O55076-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform CDK2-beta (identifier: O55076-2) The sequence of this isoform is not available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 298 | 298 | Cell division protein kinase 2 | PRO_0000085768 | |||||
Regions | |||||||||
| Domain | 4 – 286 | 283 | Protein kinase | ||||||
| Nucleotide binding | 10 – 18 | 9 | ATP By similarity | ||||||
| Nucleotide binding | 81 – 83 | 3 | ATP By similarity | ||||||
| Nucleotide binding | 129 – 132 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Active site | 127 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 33 | 1 | ATP By similarity | ||||||
| Binding site | 86 | 1 | ATP By similarity | ||||||
| Binding site | 145 | 1 | ATP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 6 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 14 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 15 | 1 | Phosphotyrosine; by WEE1 By similarity | ||||||
| Modified residue | 19 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 46 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 160 | 1 | Phosphothreonine; by CAK and CCRK By similarity | ||||||
Sequences
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References
| [1] | "The long form of CDK2 arises via alternative splicing and forms an active protein kinase with cyclins A and E." Ellenrieder C., Bartosch B., Lee G.Y., Murphy M., Sweeney C., Hergersberg M., Carrington M., Jaussi R., Hunt T. DNA Cell Biol. 20:413-423(2001) [PubMed: 11506705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| AJ223949 mRNA. Translation: CAA11680.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1H07 based on UniProtKB P24941. |
| SMR | O55076. Positions 1-298. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | O55076. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.22. 18. |
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 | CDK2_CRIGR | ||||||||
| Accession | Primary (citable) accession number: O55076 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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