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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    June 16, 2009 (Entry version 127)
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].
DOI=10.1073/pnas.88.20.9006; 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], AND VARIANT SER-290.
NIEHS SNPs program;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND SER-46, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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]
IPI IPI00031681; -.
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=1-296.[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]
2W05; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
2W06; X-ray; 2.04 A; A=1-298.[ExPASy / RCSB / EBI]
2W17; X-ray; 2.15 A; A=1-298.[ExPASy / RCSB / EBI]
2W1H; X-ray; 2.15 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]
3DOG; X-ray; 2.70 A; A/C=1-298.[ExPASy / RCSB / EBI]
3EID; X-ray; 3.15 A; A/C=1-298.[ExPASy / RCSB / EBI]
3EJ1; X-ray; 3.22 A; A/C=1-298.[ExPASy / RCSB / EBI]
3EOC; X-ray; 3.20 A; A/C=1-298.[ExPASy / RCSB / EBI]
3EZR; X-ray; 1.90 A; A=1-298.[ExPASy / RCSB / EBI]
3EZV; X-ray; 1.99 A; A=1-298.[ExPASy / RCSB / EBI]
3F5X; X-ray; 2.40 A; A/C=1-298.[ExPASy / RCSB / EBI]
3FZ1; X-ray; 1.90 A; A=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; -.
2R64; -.
2UUE; -.
2UZB; -.
2UZD; -.
2UZE; -.
2UZL; -.
2UZN; -.
2UZO; -.
2V0D; -.
2V22; -.
2VTA; -.
2VTH; -.
2VTI; -.
2VTJ; -.
2VTL; -.
2VTM; -.
2VTN; -.
2VTO; -.
2VTP; -.
2VTQ; -.
2VTR; -.
2VTS; -.
2VTT; -.
2VU3; -.
2VV9; -.
2W05; -.
2W06; -.
2W17; -.
2W1H; -.
3BHT; -.
3BHU; -.
3BHV; -.
3DDP; -.
3DDQ; -.
3DOG; -.
3EID; -.
3EJ1; -.
3EOC; -.
3EZR; -.
3EZV; -.
3F5X; -.
3FZ1; -.
ModBase P24941.
Protein-protein interaction databases
DIP DIP:161N; -.
IntAct P24941; 66.
PTM databases
PhosphoSite P24941; -.
Enzyme and pathway databases
BRENDA 2.7.11.22; 247.
Pathway_Interaction_DB bard1pathway; BARD1 signaling events.
foxm1pathway; FOXM1 transcription factor network.
foxopathway; FoxO family signaling.
il2_1pathway; IL2-mediated signaling events.
smad2_3nuclearpathway; Regulation of nuclear SMAD2/3 signaling.
prlsignalingeventspathway; Signaling events mediated by PRL.
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_383; DNA Replication.
Organism-specific databases
GeneCards GC12P054646; -.
H-InvDB HIX0010710; -.
HGNC HGNC:1771; CDK2.
GenAtlas CDK2.
HPA CAB013115; -.
MIM 116953; gene. [NCBI / EBI]
PharmGKB PA101; -.
Gene expression databases
ArrayExpress P24941; -.
Bgee 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 UniProtKB-KW).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (inferred from experiment from Reactome).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0006260; Biological process: DNA replication (inferred from experiment from Reactome).
GO:0000086; Biological process: G2/M transition of mitotic cell cycle (traceable author statement from ProtInc).
GO:0007067; Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
GO:0008284; Biological process: positive regulation of cell proliferation (traceable author statement from ProtInc).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0006275; Biological process: regulation of DNA replication (traceable author statement from ProtInc).
GO:0007089; Biological process: traversing start control point of mitotic cell cycle (traceable author statement from ProtInc).
QuickGo view.
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 of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P24941; -.
Genome annotation databases
Ensembl ENSG00000123374; Homo sapiens. [Contig view]
GeneID 1017; -.
KEGG hsa:1017; -.
Phylogenomic databases
HOGENOM P24941; -.
HOVERGEN P24941; -.
OMA P24941; GVPLRAY.
Other
BindingDB P24941; -.
NextBio 4273; -.
SOURCE CDK2; Homo sapiens.
ProtoNet P24941.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cell cycle; Cell division; Kinase; Mitosis; Nucleotide-binding; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   298  298     Cell division protein kinase 2. PRO_0000085769
DOMAIN   4   286  283     Protein kinase. 
NP_BIND   10    18  9     ATP. 
NP_BIND   81    83  3     ATP. 
NP_BIND   129   132  4     ATP. 
ACT_SITE   127   127        Proton acceptor. 
BINDING   33    33        ATP. 
BINDING   86    86        ATP. 
BINDING   145   145        ATP. 
MOD_RES   14    14        Phosphothreonine. 
MOD_RES   15    15        Phosphotyrosine; by WEE1. 
MOD_RES   19    19        Phosphotyrosine. 
MOD_RES   46    46        Phosphoserine. 
MOD_RES   160   160        Phosphothreonine; by CAK and CCRK. 
VARIANT   15    15  1     Y -> S (in dbSNP:rs3087335 [NCBI]). VAR_016157 [3D]
VARIANT   18    18  1     V -> L (in dbSNP:rs11554376 [NCBI]). VAR_053927 [3D]
VARIANT   45    45  1     P -> L (in a glioblastoma multiforme sample; somatic mutation). VAR_041972 [3D]
VARIANT   290   290  1     T -> S (in dbSNP:rs2069413 [NCBI]). VAR_019988 [3D]
MUTAGEN   14    14        T->A: 2-fold increase in activity. 
MUTAGEN   15    15        Y->F: 2-fold increase in activity. 
MUTAGEN   160   160        T->A: Abolishes activity. 
STRAND   4    12  9      
STRAND   14    23  10      
TURN   24    26  3      
STRAND   29    35  7      
HELIX   46    55  10      
STRAND   66    72  7      
STRAND   75    81  7      
STRAND   84    86  3      
HELIX   87    93  7      
TURN   94    97  4      
HELIX   101   120  20      
HELIX   130   132  3      
STRAND   133   135  3      
STRAND   141   143  3      
HELIX   148   152  5      
HELIX   171   174  4      
HELIX   183   198  16      
HELIX   208   219  12      
TURN   224   226  3      
HELIX   230   232  3      
HELIX   248   251  4      
HELIX   257   266  10      
TURN   271   273  3      
HELIX   277   281  5      
HELIX   284   286  3      
Sequence information
Length: 298 AA [This is the length of the unprocessed precursor] Molecular weight: 33930 Da [This is the MW of the unprocessed precursor] CRC64: F90A0F4E70910B51 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MENFQKVEKI GEGTYGVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH 

        70         80         90        100        110        120 
PNIVKLLDVI HTENKLYLVF EFLHQDLKKF MDASALTGIP LPLIKSYLFQ LLQGLAFCHS 

       130        140        150        160        170        180 
HRVLHRDLKP QNLLINTEGA IKLADFGLAR AFGVPVRTYT HEVVTLWYRA PEILLGCKYY 

       190        200        210        220        230        240 
STAVDIWSLG CIFAEMVTRR ALFPGDSEID QLFRIFRTLG TPDEVVWPGV TSMPDYKPSF 

       250        260        270        280        290 
PKWARQDFSK VVPPLDEDGR SLLSQMLHYD PNKRISAKAA LAHPFFQDVT KPVPHLRL 

P24941 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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