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UniProtKB/Swiss-Prot entry P24941


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDK2_HUMAN
Primary accession number P24941
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 119)
Name and origin of the protein
Protein name Cell division protein kinase 2
Synonyms EC 2.7.11.22
p33 protein kinase
Gene name
Name: CDK2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1714386 [NCBI, ExPASy, EBI, Israel, Japan]
Elledge S.J., Spottswood M.R.;
"A new human p34 protein kinase, CDK2, identified by complementation of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus Eg1.";
EMBO J. 10:2653-2659(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/353174a0; PubMed=1653904 [NCBI, ExPASy, EBI, Israel, Japan]
Tsai L.-H., Harlow E., Meyerson M.;
"Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase.";
Nature 353:174-177(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1717994 [NCBI, ExPASy, EBI, Israel, Japan]
Ninomiya-Tsuji J., Nomoto S., Yasuda H., Reed S.I., Matsumoto K.;
"Cloning of a human cDNA encoding a CDC2-related kinase by complementation of a budding yeast cdc28 mutation.";
Proc. Natl. Acad. Sci. U.S.A. 88:9006-9010(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160, AND MUTAGENESIS OF THR-14; TYR-15 AND THR-160.
PubMed=1396589 [NCBI, ExPASy, EBI, Israel, Japan]
Gu Y., Rosenblatt J., O'Morgan D.O.;
"Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15.";
EMBO J. 11:3995-4005(1992).
[8]
INTERACTION WITH CCNB3.
DOI=10.1074/jbc.M203951200; PubMed=12185076 [NCBI, ExPASy, EBI, Israel, Japan]
Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S., Wang X.-Y., Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.;
"Characterization and expression of mammalian cyclin b3, a prepachytene meiotic cyclin.";
J. Biol. Chem. 277:41960-41969(2002).
[9]
INTERACTION WITH SPDYA.
DOI=10.1083/jcb.200109045; PubMed=11980914 [NCBI, ExPASy, EBI, Israel, Japan]
Porter L.A., Dellinger R.W., Tynan J.A., Barnes E.A., Kong M., Lenormand J.-L., Donoghue D.J.;
"Human Speedy: a novel cell cycle regulator that enhances proliferation through activation of Cdk2.";
J. Cell Biol. 157:357-366(2002).
[10]
INTERACTION WITH SPDYA.
PubMed=12839962 [NCBI, ExPASy, EBI, Israel, Japan]
Barnes E.A., Porter L.A., Lenormand J.-L., Dellinger R.W., Donoghue D.J.;
"Human Spy1 promotes survival of mammalian cells following DNA damage.";
Cancer Res. 63:3701-3707(2003).
[11]
INTERACTION WITH SPDYA, AND IDENTIFICATION IN A COMPLEX WITH CDKN1B AND SPDYA.
DOI=10.1091/mbc.E02-12-0820; PubMed=12972555 [NCBI, ExPASy, EBI, Israel, Japan]
Porter L.A., Kong-Beltran M., Donoghue D.J.;
"Spy1 interacts with p27Kip1 to allow G1/S progression.";
Mol. Biol. Cell 14:3664-3674(2003).
[12]
INTERACTION WITH UHRF2, AND IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CCNE1.
DOI=10.1016/j.bbrc.2004.04.190; PubMed=15178429 [NCBI, ExPASy, EBI, Israel, Japan]
Li Y., Mori T., Hata H., Homma Y., Kochi H.;
"NIRF induces G1 arrest and associates with Cdk2.";
Biochem. Biophys. Res. Commun. 319:464-468(2004).
[13]
PHOSPHORYLATION AT THR-160.
DOI=10.1074/jbc.M309995200; PubMed=14597612 [NCBI, ExPASy, EBI, Israel, Japan]
Liu Y., Wu C., Galaktionov K.;
"p42, a novel cyclin-dependent kinase-activating kinase in mammalian cells.";
J. Biol. Chem. 279:4507-4514(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[15]
INTERACTION WITH SPDYA AND SPDYC.
PubMed=15611625 [NCBI, ExPASy, EBI, Israel, Japan]
Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.;
"Identification and comparative analysis of multiple mammalian Speedy/Ringo proteins.";
Cell Cycle 4:155-165(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASS SPECTROMETRY.
TISSUE=Lung;
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15; TYR-19 AND THR-160, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[18]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1038/363595a0; PubMed=8510751 [NCBI, ExPASy, EBI, Israel, Japan]
de Bondt H.L., Rosenblatt J., Jancarik J., Jones H.D., Morgan D.O., Kim S.-H.;
"Crystal structure of cyclin-dependent kinase 2.";
Nature 363:595-602(1993).
[19]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CYCLIN A.
DOI=10.1038/376313a0; PubMed=7630397 [NCBI, ExPASy, EBI, Israel, Japan]
Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., Pavletich N.P.;
"Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.";
Nature 376:313-320(1995).
[20]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITG CKS1.
DOI=10.1016/S0092-8674(00)81065-X; PubMed=8601310 [NCBI, ExPASy, EBI, Israel, Japan]
Bourne Y., Watson M.H., Hickey M.J., Holmes W., Rocque W., Reed S.I., Tainer J.A.;
"Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1.";
Cell 84:863-874(1996).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
DOI=10.1021/jm960402a; PubMed=8917641 [NCBI, ExPASy, EBI, Israel, Japan]
Schulze-Gahmen U., de Bondt H.L., Kim S.-H.;
"High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design.";
J. Med. Chem. 39:4540-4546(1996).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CG2A AND KIP1.
DOI=10.1038/382325a0; PubMed=8684460 [NCBI, ExPASy, EBI, Israel, Japan]
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.;
"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex.";
Nature 382:325-331(1996).
[23]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH CG2A.
DOI=10.1038/nsb0896-696; PubMed=8756328 [NCBI, ExPASy, EBI, Israel, Japan]
Russo A.A., Jeffrey P.D., Pavletich N.P.;
"Structural basis of cyclin-dependent kinase activation by phosphorylation.";
Nat. Struct. Biol. 3:696-700(1996).
[24]
X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF COMPLEX WITH L868276.
DOI=10.1073/pnas.93.7.2735; PubMed=8610110 [NCBI, ExPASy, EBI, Israel, Japan]
de Azevedo W.F. Jr., Mueller-Dieckmann H.-J., Schulze-Gahmen U., Worland P.J., Sausville E., Kim S.-H.;
"Structural basis for specificity and potency of a flavonoid inhibitor of human CDK2, a cell cycle kinase.";
Proc. Natl. Acad. Sci. U.S.A. 93:2735-2740(1996).
[25]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1038/nsb1097-796; PubMed=9334743 [NCBI, ExPASy, EBI, Israel, Japan]
Lawrie A.M., Noble M.E.M., Tunnah P., Brown N.R., Johnson L.N., Endicott J.A.;
"Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2.";
Nat. Struct. Biol. 4:796-801(1997).
[26]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
DOI=10.1126/science.281.5376.533; PubMed=9677190 [NCBI, ExPASy, EBI, Israel, Japan]
Gray N.S., Wodicka L., Thunnissen A.-M.W.H., Norman T.C., Kwon S., Espinoza F.H., Morgan D.O., Barnes G., Leclerc S., Meijer L., Kim S.H., Lockhart D.J., Schultz P.G.;
"Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors.";
Science 281:533-538(1998).
[27]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-288 IN COMPLEX WITH CCNB1, AND FUNCTION.
PubMed=17495531 [NCBI, ExPASy, EBI, Israel, Japan]
Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.;
"Cyclin B and cyclin A confer different substrate recognition properties on CDK2.";
Cell Cycle 6:1350-1359(2007).
[28]
VARIANTS [LARGE SCALE ANALYSIS] LEU-45 AND SER-290.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X61622; CAA43807.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X62071; CAA43985.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68520; AAA35667.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006821; AAP35467.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF512553; AAM34794.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003065; AAH03065.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41227; A41227.
RefSeq NP_001789.2; -.
UniGene Hs.19192
3D structure databases
PDB
1AQ1; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1B38; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1B39; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
1BUH; X-ray; 2.60 A; A=1-298.[ExPASy / RCSB / EBI]
1CKP; X-ray; 2.05 A; A=1-298.[ExPASy / RCSB / EBI]
1DI8; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1DM2; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
1E1V; X-ray; 1.95 A; A=1-298.[ExPASy / RCSB / EBI]
1E1X; X-ray; 1.85 A; A=1-298.[ExPASy / RCSB / EBI]
1E9H; X-ray; 2.50 A; A/C=1-296.[ExPASy / RCSB / EBI]
1F5Q; X-ray; 2.50 A; A/C=1-298.[ExPASy / RCSB / EBI]
1FIN; X-ray; 2.30 A; A/C=1-298.[ExPASy / RCSB / EBI]
1FQ1; X-ray; 3.00 A; B=1-298.[ExPASy / RCSB / EBI]
1FVT; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1FVV; X-ray; 2.80 A; A/C=1-298.[ExPASy / RCSB / EBI]
1G5S; X-ray; 2.61 A; A=1-298.[ExPASy / RCSB / EBI]
1GIH; X-ray; 2.80 A; A=1-298.[ExPASy / RCSB / EBI]
1GII; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1GIJ; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1GY3; X-ray; 2.70 A; A/C=1-298.[ExPASy / RCSB / EBI]
1GZ8; X-ray; 1.30 A; A=1-298.[ExPASy / RCSB / EBI]
1H00; X-ray; 1.60 A; A=1-298.[ExPASy / RCSB / EBI]
1H01; X-ray; 1.79 A; A=1-298.[ExPASy / RCSB / EBI]
1H07; X-ray; 1.85 A; A=1-298.[ExPASy / RCSB / EBI]
1H08; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
1H0V; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
1H0W; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
1H1P; X-ray; 2.10 A; A/C=1-298.[ExPASy / RCSB / EBI]
1H1Q; X-ray; 2.50 A; A/C=1-298.[ExPASy / RCSB / EBI]
1H1R; X-ray; 2.00 A; A/C=1-298.[ExPASy / RCSB / EBI]
1H1S; X-ray; 2.00 A; A/C=1-298.[ExPASy / RCSB / EBI]
1H24; X-ray; 2.50 A; A/C=1-298.[ExPASy / RCSB / EBI]
1H25; X-ray; 2.50 A; A/C=1-298.[ExPASy / RCSB / EBI]
1H26; X-ray; 2.24 A; A/C=1-298.[ExPASy / RCSB / EBI]
1H27; X-ray; 2.20 A; A/C=1-298.[ExPASy / RCSB / EBI]
1H28; X-ray; 2.80 A; A/C=1-298.[ExPASy / RCSB / EBI]
1HCK; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
1HCL; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
1JST; X-ray; 2.60 A; A/C=1-298.[ExPASy / RCSB / EBI]
1JSU; X-ray; 2.30 A; A=1-298.[ExPASy / RCSB / EBI]
1JSV; X-ray; 1.96 A; A=1-298.[ExPASy / RCSB / EBI]
1JVP; X-ray; 1.53 A; P=1-298.[ExPASy / RCSB / EBI]
1KE5; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1KE6; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1KE7; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1KE8; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1KE9; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1OGU; X-ray; 2.60 A; A/C=1-298.[ExPASy / RCSB / EBI]
1OI9; X-ray; 2.10 A; A/C=1-298.[ExPASy / RCSB / EBI]
1OIQ; X-ray; 2.31 A; A=1-298.[ExPASy / RCSB / EBI]
1OIR; X-ray; 1.91 A; A=1-298.[ExPASy / RCSB / EBI]
1OIT; X-ray; 1.60 A; A=1-298.[ExPASy / RCSB / EBI]
1OIU; X-ray; 2.00 A; A/C=1-298.[ExPASy / RCSB / EBI]
1OIY; X-ray; 2.40 A; A/C=1-298.[ExPASy / RCSB / EBI]
1OKV; X-ray; 2.40 A; A/C=1-298.[ExPASy / RCSB / EBI]
1OKW; X-ray; 2.50 A; A/C=1-298.[ExPASy / RCSB / EBI]
1OL1; X-ray; 2.90 A; A/C=1-298.[ExPASy / RCSB / EBI]
1OL2; X-ray; 2.60 A; A/C=1-298.[ExPASy / RCSB / EBI]
1P2A; X-ray; 2.50 A; A=1-298.[ExPASy / RCSB / EBI]
1P5E; X-ray; 2.22 A; A/C=1-298.[ExPASy / RCSB / EBI]
1PF8; X-ray; 2.51 A; A=1-298.[ExPASy / RCSB / EBI]
1PKD; X-ray; 2.30 A; A/C=1-296.[ExPASy / RCSB / EBI]
1PW2; X-ray; 1.95 A; A=1-298.[ExPASy / RCSB / EBI]
1PXI; X-ray; 1.95 A; A=1-298.[ExPASy / RCSB / EBI]
1PXJ; X-ray; 2.30 A; A=1-298.[ExPASy / RCSB / EBI]
1PXK; X-ray; 2.80 A; A=1-298.[ExPASy / RCSB / EBI]
1PXL; X-ray; 2.50 A; A=1-298.[ExPASy / RCSB / EBI]
1PXM; X-ray; 2.53 A; A=1-298.[ExPASy / RCSB / EBI]
1PXN; X-ray; 2.50 A; A=1-298.[ExPASy / RCSB / EBI]
1PXO; X-ray; 1.96 A; A=1-298.[ExPASy / RCSB / EBI]
1PXP; X-ray; 2.30 A; A=1-298.[ExPASy / RCSB / EBI]
1PYE; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1QMZ; X-ray; 2.20 A; A/C=1-298.[ExPASy / RCSB / EBI]
1R78; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1URC; X-ray; 2.60 A; A/C=1-298.[ExPASy / RCSB / EBI]
1URW; X-ray; 1.60 A; A=1-298.[ExPASy / RCSB / EBI]
1V1K; X-ray; 2.31 A; A=1-298.[ExPASy / RCSB / EBI]
1VYW; X-ray; 2.30 A; A/C=1-298.[ExPASy / RCSB / EBI]
1VYZ; X-ray; 2.21 A; A=1-298.[ExPASy / RCSB / EBI]
1W0X; X-ray; 2.20 A; C=1-298.[ExPASy / RCSB / EBI]
1W8C; X-ray; 2.05 A; A=1-298.[ExPASy / RCSB / EBI]
1W98; X-ray; 2.15 A; A=1-297.[ExPASy / RCSB / EBI]
1WCC; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
1Y8Y; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
1Y91; X-ray; 2.15 A; A=1-298.[ExPASy / RCSB / EBI]
1YKR; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
2A0C; X-ray; 1.95 A; X=1-298.[ExPASy / RCSB / EBI]
2A4L; X-ray; 2.40 A; A=1-298.[ExPASy / RCSB / EBI]
2B52; X-ray; 1.88 A; A=1-298.[ExPASy / RCSB / EBI]
2B53; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
2B54; X-ray; 1.85 A; A=1-298.[ExPASy / RCSB / EBI]
2B55; X-ray; 1.85 A; A=1-298.[ExPASy / RCSB / EBI]
2BHE; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2BHH; X-ray; 2.60 A; A=1-298.[ExPASy / RCSB / EBI]
2BKZ; X-ray; 2.60 A; A/C=1-298.[ExPASy / RCSB / EBI]
2BPM; X-ray; 2.40 A; A/C=1-298.[ExPASy / RCSB / EBI]
2BTR; X-ray; 1.85 A; A=1-298.[ExPASy / RCSB / EBI]
2BTS; X-ray; 1.99 A; A=1-298.[ExPASy / RCSB / EBI]
2C4G; X-ray; 2.70 A; A/C=1-298.[ExPASy / RCSB / EBI]
2C5N; X-ray; 2.10 A; A/C=1-298.[ExPASy / RCSB / EBI]
2C5O; X-ray; 2.10 A; A/C=1-298.[ExPASy / RCSB / EBI]
2C5P; X-ray; 2.30 A; A/C=1-298.[ExPASy / RCSB / EBI]
2C5V; X-ray; 2.90 A; A/C=1-298.[ExPASy / RCSB / EBI]
2C5X; X-ray; 2.90 A; A/C=1-298.[ExPASy / RCSB / EBI]
2C5Y; X-ray; 2.25 A; A=1-298.[ExPASy / RCSB / EBI]
2C68; X-ray; 1.95 A; A=1-298.[ExPASy / RCSB / EBI]
2C69; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
2C6I; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
2C6K; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2C6L; X-ray; 2.30 A; A=1-298.[ExPASy / RCSB / EBI]
2C6M; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2C6O; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
2C6T; X-ray; 2.61 A; A/C=1-298.[ExPASy / RCSB / EBI]
2CCH; X-ray; 1.70 A; A/C=1-298.[ExPASy / RCSB / EBI]
2CCI; X-ray; 2.70 A; A/C=1-298.[ExPASy / RCSB / EBI]
2CJM; X-ray; 2.30 A; A/C=1-298.[ExPASy / RCSB / EBI]
2CLX; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
2DS1; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
2DUV; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
2EXM; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
2FVD; X-ray; 1.85 A; A=1-298.[ExPASy / RCSB / EBI]
2G9X; X-ray; 2.50 A; A/C=1-298.[ExPASy / RCSB / EBI]
2HIC; Model; -; A=1-298.[ExPASy / RCSB / EBI]
2I40; X-ray; 2.80 A; A/C=1-298.[ExPASy / RCSB / EBI]
2IW6; X-ray; 2.30 A; A/C=1-298.[ExPASy / RCSB / EBI]
2IW8; X-ray; 2.30 A; A/C=1-298.[ExPASy / RCSB / EBI]
2IW9; X-ray; 2.00 A; A/C=1-298.[ExPASy / RCSB / EBI]
2J9M; X-ray; 2.50 A; A=1-298.[ExPASy / RCSB / EBI]
2JGZ; X-ray; 2.90 A; A=1-288.[ExPASy / RCSB / EBI]
2R3F; X-ray; 1.50 A; A=1-298.[ExPASy / RCSB / EBI]
2R3G; X-ray; 1.55 A; A=1-298.[ExPASy / RCSB / EBI]
2R3H; X-ray; 1.50 A; A=1-298.[ExPASy / RCSB / EBI]
2R3I; X-ray; 1.28 A; A=1-298.[ExPASy / RCSB / EBI]
2R3J; X-ray; 1.65 A; A=1-298.[ExPASy / RCSB / EBI]
2R3K; X-ray; 1.70 A; A=1-298.[ExPASy / RCSB / EBI]
2R3L; X-ray; 1.65 A; A=1-298.[ExPASy / RCSB / EBI]
2R3M; X-ray; 1.70 A; A=1-298.[ExPASy / RCSB / EBI]
2R3N; X-ray; 1.63 A; A=1-298.[ExPASy / RCSB / EBI]
2R3O; X-ray; 1.80 A; A=1-298.[ExPASy / RCSB / EBI]
2R3P; X-ray; 1.66 A; A=1-298.[ExPASy / RCSB / EBI]
2R3Q; X-ray; 1.35 A; A=1-298.[ExPASy / RCSB / EBI]
2R3R; X-ray; 1.47 A; A=1-298.[ExPASy / RCSB / EBI]
2R64; X-ray; 2.30 A; A=1-298.[ExPASy / RCSB / EBI]
2UUE; X-ray; 2.06 A; A/C=1-298.[ExPASy / RCSB / EBI]
2UZB; X-ray; 2.70 A; A/C=1-298.[ExPASy / RCSB / EBI]
2UZD; X-ray; 2.72 A; A/C=1-298.[ExPASy / RCSB / EBI]
2UZE; X-ray; 2.40 A; A/C=1-298.[ExPASy / RCSB / EBI]
2UZL; X-ray; 2.40 A; A/C=1-298.[ExPASy / RCSB / EBI]
2UZN; X-ray; 2.30 A; A=1-298.[ExPASy / RCSB / EBI]
2UZO; X-ray; 2.30 A; A=1-298.[ExPASy / RCSB / EBI]
2V0D; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
2V22; X-ray; 2.60 A; A/C=1-298.[ExPASy / RCSB / EBI]
2VTA; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
2VTH; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2VTI; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
2VTJ; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
2VTL; X-ray; 2.00 A; A=1-298.[ExPASy / RCSB / EBI]
2VTM; X-ray; 2.25 A; A=1-298.[ExPASy / RCSB / EBI]
2VTN; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
2VTO; X-ray; 2.19 A; A=1-298.[ExPASy / RCSB / EBI]
2VTP; X-ray; 2.15 A; A=1-298.[ExPASy / RCSB / EBI]
2VTQ; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2VTR; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2VTS; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2VTT; X-ray; 1.68 A; A=1-298.[ExPASy / RCSB / EBI]
2VU3; X-ray; 1.85 A; A=1-298.[ExPASy / RCSB / EBI]
2VV9; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2W06; X-ray; 2.04 A; A=1-298.[ExPASy / RCSB / EBI]
3BHT; X-ray; 2.00 A; A/C=1-298.[ExPASy / RCSB / EBI]
3BHU; X-ray; 2.30 A; A/C=1-298.[ExPASy / RCSB / EBI]
3BHV; X-ray; 2.10 A; A/C=1-298.[ExPASy / RCSB / EBI]
3DDP; X-ray; 2.70 A; A/C=1-298.[ExPASy / RCSB / EBI]
3DDQ; X-ray; 1.80 A; A/C=1-298.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AQ1; -.
1B38; -.
1B39; -.
1BUH; -.
1CKP; -.
1DI8; -.
1DM2; -.
1E1V; -.
1E1X; -.
1E9H; -.
1F5Q; -.
1FIN; -.
1FQ1; -.
1FVT; -.
1FVV; -.
1G5S; -.
1GIH; -.
1GII; -.
1GIJ; -.
1GY3; -.
1GZ8; -.
1H00; -.
1H01; -.
1H07; -.
1H08; -.
1H0V; -.
1H0W; -.
1H1P; -.
1H1Q; -.
1H1R; -.
1H1S; -.
1H24; -.
1H25; -.
1H26; -.
1H27; -.
1H28; -.
1HCK; -.
1HCL; -.
1JST; -.
1JSU; -.
1JSV; -.
1JVP; -.
1KE5; -.
1KE6; -.
1KE7; -.
1KE8; -.
1KE9; -.
1OGU; -.
1OI9; -.
1OIQ; -.
1OIR; -.
1OIT; -.
1OIU; -.
1OIY; -.
1OKV; -.
1OKW; -.
1OL1; -.
1OL2; -.
1P2A; -.
1P5E; -.
1PF8; -.
1PKD; -.
1PW2; -.
1PXI; -.
1PXJ; -.
1PXK; -.
1PXL; -.
1PXM; -.
1PXN; -.
1PXO; -.
1PXP; -.
1PYE; -.
1QMZ; -.
1R78; -.
1URC; -.
1URW; -.
1V1K; -.
1VYW; -.
1VYZ; -.
1W0X; -.
1W8C; -.
1W98; -.
1WCC; -.
1Y8Y; -.
1Y91; -.
1YKR; -.
2A0C; -.
2A4L; -.
2B52; -.
2B53; -.
2B54; -.
2B55; -.
2BHE; -.
2BHH; -.
2BKZ; -.
2BPM; -.
2BTR; -.
2BTS; -.
2C4G; -.
2C5N; -.
2C5O; -.
2C5P; -.
2C5V; -.
2C5X; -.
2C5Y; -.
2C68; -.
2C69; -.
2C6I; -.
2C6K; -.
2C6L; -.
2C6M; -.
2C6O; -.
2C6T; -.
2CCH; -.
2CCI; -.
2CJM; -.
2CLX; -.
2DS1; -.
2DUV; -.
2EXM; -.
2FVD; -.
2G9X; -.
2HIC; -.
2I40; -.
2IW6; -.
2IW8; -.
2IW9; -.
2J9M; -.
2JGZ; -.
2R3F; -.
2R3G; -.
2R3H; -.
2R3I; -.
2R3J; -.
2R3K; -.
2R3L; -.
2R3M; -.
2R3N; -.
2R3O; -.
2R3P; -.
2R3Q; -.
2R3R; -.
2UUE; -.
2UZB; -.
2UZD; -.
2UZE; -.
2UZL; -.
2UZN; -.
2UZO; -.
2V0D; -.
2V22; -.
2VTA; -.
2VTH; -.
2VTI; -.
2VTJ; -.
2VTL; -.
2VTM; -.
2VTN; -.
2VTO; -.
2VTP; -.
2VTQ; -.
2VTR; -.
2VTS; -.
2VTT; -.
2VU3; -.
2VV9; -.
3BHT; -.
3BHU; -.
3BHV; -.
3DDP; -.
3DDQ; -.
ModBase P24941.
Protein-protein interaction databases
DIP DIP:161N; -.
IntAct P24941; -.
PTM databases
PhosphoSite P24941; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
Polymorphism databases
NIEHS-SNPs CDK2.
Organism-specific databases
H-InvDB HIX0010710; -.
HGNC HGNC:1771; CDK2.
GenAtlas CDK2.
HPA CAB013115; -.
MIM 116953; gene. [NCBI / EBI]
PharmGKB PA101; -.
GeneCards P24941.
Gene expression databases
ArrayExpress P24941; -.
CleanEx HS_CDK2; -.
GermOnline ENSG00000123374; Homo sapiens.
Ontologies
GO
GO:0000307; Cellular component: cyclin-dependent protein kinase holoenzyme complex (inferred from direct assay from UniProtKB).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (traceable author statement from ProtInc).
GO:0042802;