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Reviewed, UniProtKB/Swiss-Prot P24941 (CDK2_HUMAN)

Last modified February 9, 2010. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cell division protein kinase 2
    EC=2.7.11.22
Alternative name(s):
    p33 protein kinase
Gene names
Name: CDK2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.35

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.

Subunit structure

Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts with CABLES1 By similarity. 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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Cell division protein kinase 2
PRO_0000085769

Regions

Domain4 – 286283Protein kinase
Nucleotide binding10 – 189ATP
Nucleotide binding81 – 833ATP
Nucleotide binding129 – 1324ATP

Sites

Active site1271Proton acceptor
Binding site331ATP
Binding site861ATP
Binding site1451ATP

Amino acid modifications

Modified residue61N6-acetyllysine Ref.25
Modified residue141Phosphothreonine Ref.9 Ref.16 Ref.19
Modified residue151Phosphotyrosine; by WEE1 Ref.9 Ref.19 Ref.18 Ref.20 Ref.22 Ref.24
Modified residue191Phosphotyrosine Ref.19 Ref.18
Modified residue461Phosphoserine Ref.20
Modified residue1581Phosphothreonine
Modified residue1591Phosphotyrosine
Modified residue1601Phosphothreonine; by CAK and CCRK Ref.9 Ref.19 Ref.24 Ref.15

Natural variations

Natural variant151Y → S: dbSNP rs3087335.
VAR_016157
Natural variant181V → L: dbSNP rs11554376.
VAR_053927
Natural variant451P → L in a glioblastoma multiforme sample; somatic mutation. Ref.36
VAR_041972
Natural variant2901T → S: dbSNP rs2069413. Ref.36 Ref.5
VAR_019988

Experimental info

Mutagenesis141T → A: 2-fold increase in activity. Ref.9
Mutagenesis151Y → F: 2-fold increase in activity. Ref.9
Mutagenesis1601T → A: Abolishes activity. Ref.9

Secondary structure

............................................... 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24941-1 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: F90A0F4E70910B51

FASTA29833,930
        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 

« Hide

References

« Hide 'large scale' references
[1]"A new human p34 protein kinase, CDK2, identified by complementation of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus Eg1."
Elledge S.J., Spottswood M.R.
EMBO J. 10:2653-2659(1991) [PubMed: 1714386] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase."
Tsai L.-H., Harlow E., Meyerson M.
Nature 353:174-177(1991) [PubMed: 1653904] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of a human cDNA encoding a CDC2-related kinase by complementation of a budding yeast cdc28 mutation."
Ninomiya-Tsuji J., Nomoto S., Yasuda H., Reed S.I., Matsumoto K.
Proc. Natl. Acad. Sci. U.S.A. 88:9006-9010(1991) [PubMed: 1717994] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIEHS SNPs program
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-290.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[9]"Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15."
Gu Y., Rosenblatt J., O'Morgan D.O.
EMBO J. 11:3995-4005(1992) [PubMed: 1396589] [Abstract]
Cited for: PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160, MUTAGENESIS OF THR-14; TYR-15 AND THR-160.
[10]"Characterization and expression of mammalian cyclin b3, a prepachytene meiotic cyclin."
Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S., Wang X.-Y., Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.
J. Biol. Chem. 277:41960-41969(2002) [PubMed: 12185076] [Abstract]
Cited for: INTERACTION WITH CCNB3.
[11]"Human Speedy: a novel cell cycle regulator that enhances proliferation through activation of Cdk2."
Porter L.A., Dellinger R.W., Tynan J.A., Barnes E.A., Kong M., Lenormand J.-L., Donoghue D.J.
J. Cell Biol. 157:357-366(2002) [PubMed: 11980914] [Abstract]
Cited for: INTERACTION WITH SPDYA.
[12]"Human Spy1 promotes survival of mammalian cells following DNA damage."
Barnes E.A., Porter L.A., Lenormand J.-L., Dellinger R.W., Donoghue D.J.
Cancer Res. 63:3701-3707(2003) [PubMed: 12839962] [Abstract]
Cited for: INTERACTION WITH SPDYA.
[13]"Spy1 interacts with p27Kip1 to allow G1/S progression."
Porter L.A., Kong-Beltran M., Donoghue D.J.
Mol. Biol. Cell 14:3664-3674(2003) [PubMed: 12972555] [Abstract]
Cited for: INTERACTION WITH SPDYA, IDENTIFICATION IN A COMPLEX WITH CDKN1B AND SPDYA.
[14]"NIRF induces G1 arrest and associates with Cdk2."
Li Y., Mori T., Hata H., Homma Y., Kochi H.
Biochem. Biophys. Res. Commun. 319:464-468(2004) [PubMed: 15178429] [Abstract]
Cited for: INTERACTION WITH UHRF2, IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CCNE1.
[15]"p42, a novel cyclin-dependent kinase-activating kinase in mammalian cells."
Liu Y., Wu C., Galaktionov K.
J. Biol. Chem. 279:4507-4514(2004) [PubMed: 14597612] [Abstract]
Cited for: PHOSPHORYLATION AT THR-160.
[16]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14, MASS SPECTROMETRY.
Tissue: Epithelium.
[17]"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 AND SPDYC.
[18]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
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. expand/collapse author list , 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.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, MASS SPECTROMETRY.
Tissue: Lung.
[19]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15; TYR-19 AND THR-160, MASS SPECTROMETRY.
[20]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND SER-46, MASS SPECTROMETRY.
[21]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[22]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[23]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15; TYR-19; SER-46; THR-158 AND TYR-159, MASS SPECTROMETRY.
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND THR-160, MASS SPECTROMETRY.
Tissue: T-cell.
[25]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6, MASS SPECTROMETRY.
[26]"Crystal structure of cyclin-dependent kinase 2."
de Bondt H.L., Rosenblatt J., Jancarik J., Jones H.D., Morgan D.O., Kim S.-H.
Nature 363:595-602(1993) [PubMed: 8510751] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[27]"Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex."
Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., Pavletich N.P.
Nature 376:313-320(1995) [PubMed: 7630397] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CYCLIN A.
[28]"Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1."
Bourne Y., Watson M.H., Hickey M.J., Holmes W., Rocque W., Reed S.I., Tainer J.A.
Cell 84:863-874(1996) [PubMed: 8601310] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITG CKS1.
[29]"High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design."
Schulze-Gahmen U., de Bondt H.L., Kim S.-H.
J. Med. Chem. 39:4540-4546(1996) [PubMed: 8917641] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[30]"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex."
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.
Nature 382:325-331(1996) [PubMed: 8684460] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CG2A AND KIP1.
[31]"Structural basis of cyclin-dependent kinase activation by phosphorylation."
Russo A.A., Jeffrey P.D., Pavletich N.P.
Nat. Struct. Biol. 3:696-700(1996) [PubMed: 8756328] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH CG2A.
[32]"Structural basis for specificity and potency of a flavonoid inhibitor of human CDK2, a cell cycle kinase."
de Azevedo W.F. Jr., Mueller-Dieckmann H.-J., Schulze-Gahmen U., Worland P.J., Sausville E., Kim S.-H.
Proc. Natl. Acad. Sci. U.S.A. 93:2735-2740(1996) [PubMed: 8610110] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF COMPLEX WITH L868276.
[33]"Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2."
Lawrie A.M., Noble M.E.M., Tunnah P., Brown N.R., Johnson L.N., Endicott J.A.
Nat. Struct. Biol. 4:796-801(1997) [PubMed: 9334743] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[34]"Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors."
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.
Science 281:533-538(1998) [PubMed: 9677190] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
[35]"Cyclin B and cyclin A confer different substrate recognition properties on CDK2."
Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.
Cell Cycle 6:1350-1359(2007) [PubMed: 17495531] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-288 IN COMPLEX WITH CCNB1, FUNCTION.
[36]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-45 AND SER-290.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61622 mRNA. Translation: CAA43807.1.
X62071 mRNA. Translation: CAA43985.1.
M68520 mRNA. Translation: AAA35667.1.
BT006821 mRNA. Translation: AAP35467.1.
AF512553 Genomic DNA. Translation: AAM34794.1.
AK291941 mRNA. Translation: BAF84630.1.
CH471054 Genomic DNA. Translation: EAW96858.1.
BC003065 mRNA. Translation: AAH03065.1.
IPIIPI00031681.
PIRA41227.
RefSeqNP_001789.2.
NP_439892.2.
UniGeneHs.19192
Hs.689624

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQ1X-ray2.00A1-298[»]
1B38X-ray2.00A1-298[»]
1B39X-ray2.10A1-298[»]
1BUHX-ray2.60A1-298[»]
1CKPX-ray2.05A1-298[»]
1DI8X-ray2.20A1-298[»]
1DM2X-ray2.10A1-298[»]
1E1VX-ray1.95A1-298[»]
1E1XX-ray1.85A1-298[»]
1E9HX-ray2.50A/C1-296[»]
1F5QX-ray2.50A/C1-298[»]
1FINX-ray2.30A/C1-298[»]
1FQ1X-ray3.00B1-298[»]
1FVTX-ray2.20A1-298[»]
1FVVX-ray2.80A/C1-298[»]
1G5SX-ray2.61A1-298[»]
1GIHX-ray2.80A1-298[»]
1GIIX-ray2.00A1-298[»]
1GIJX-ray2.20A1-298[»]
1GY3X-ray2.70A/C1-296[»]
1GZ8X-ray1.30A1-298[»]
1H00X-ray1.60A1-298[»]
1H01X-ray1.79A1-298[»]
1H07X-ray1.85A1-298[»]
1H08X-ray1.80A1-298[»]
1H0VX-ray1.90A1-298[»]
1H0WX-ray2.10A1-298[»]
1H1PX-ray2.10A/C1-298[»]
1H1QX-ray2.50A/C1-298[»]
1H1RX-ray2.00A/C1-298[»]
1H1SX-ray2.00A/C1-298[»]
1H24X-ray2.50A/C1-298[»]
1H25X-ray2.50A/C1-298[»]
1H26X-ray2.24A/C1-298[»]
1H27X-ray2.20A/C1-298[»]
1H28X-ray2.80A/C1-298[»]
1HCKX-ray1.90A1-298[»]
1HCLX-ray1.80A1-298[»]
1JSTX-ray2.60A/C1-298[»]
1JSUX-ray2.30A1-298[»]
1JSVX-ray1.96A1-298[»]
1JVPX-ray1.53P1-298[»]
1KE5X-ray2.20A1-298[»]
1KE6X-ray2.00A1-298[»]
1KE7X-ray2.00A1-298[»]
1KE8X-ray2.00A1-298[»]
1KE9X-ray2.00A1-298[»]
1OGUX-ray2.60A/C1-298[»]
1OI9X-ray2.10A/C1-298[»]
1OIQX-ray2.31A1-298[»]
1OIRX-ray1.91A1-298[»]
1OITX-ray1.60A1-298[»]
1OIUX-ray2.00A/C1-298[»]
1OIYX-ray2.40A/C1-298[»]
1OKVX-ray2.40A/C1-298[»]
1OKWX-ray2.50A/C1-298[»]
1OL1X-ray2.90A/C1-298[»]
1OL2X-ray2.60A/C1-298[»]
1P2AX-ray2.50A1-298[»]
1P5EX-ray2.22A/C1-298[»]
1PF8X-ray2.51A1-298[»]
1PKDX-ray2.30A/C1-296[»]
1PW2X-ray1.95A1-298[»]
1PXIX-ray1.95A1-298[»]
1PXJX-ray2.30A1-298[»]
1PXKX-ray2.80A1-298[»]
1PXLX-ray2.50A1-298[»]
1PXMX-ray2.53A1-298[»]
1PXNX-ray2.50A1-298[»]
1PXOX-ray1.96A1-298[»]
1PXPX-ray2.30A1-298[»]
1PYEX-ray2.00A1-298[»]
1QMZX-ray2.20A/C1-298[»]
1R78X-ray2.00A1-298[»]
1URCX-ray2.60A/C1-298[»]
1URWX-ray1.60A1-298[»]
1V1KX-ray2.31A1-298[»]
1VYWX-ray2.30A/C1-298[»]
1VYZX-ray2.21A1-298[»]
1W0XX-ray2.20C1-298[»]
1W8CX-ray2.05A1-298[»]
1W98X-ray2.15A1-297[»]
1WCCX-ray2.20A1-298[»]
1Y8YX-ray2.00A1-298[»]
1Y91X-ray2.15A1-298[»]
1YKRX-ray1.80A1-298[»]
2A0CX-ray1.95X1-298[»]
2A4LX-ray2.40A1-298[»]
2B52X-ray1.88A1-298[»]
2B53X-ray2.00A1-298[»]
2B54X-ray1.85A1-298[»]
2B55X-ray1.85A1-298[»]
2BHEX-ray1.90A1-298[»]
2BHHX-ray2.60A1-298[»]
2BKZX-ray2.60A/C1-298[»]
2BPMX-ray2.40A/C1-298[»]
2BTRX-ray1.85A1-298[»]
2BTSX-ray1.99A1-298[»]
2C4GX-ray2.70A/C1-298[»]
2C5NX-ray2.10A/C1-298[»]
2C5OX-ray2.10A/C1-298[»]
2C5VX-ray2.90A/C1-298[»]
2C5XX-ray2.90A/C1-298[»]
2C5YX-ray2.25A1-298[»]
2C68X-ray1.95A1-298[»]
2C69X-ray2.10A1-298[»]
2C6IX-ray1.80A1-298[»]
2C6KX-ray1.90A1-298[»]
2C6LX-ray2.30A1-298[»]
2C6MX-ray1.90A1-298[»]
2C6OX-ray2.10A1-298[»]
2C6TX-ray2.61A/C1-298[»]
2CCHX-ray1.70A/C1-298[»]
2CCIX-ray2.70A/C1-298[»]
2CJMX-ray2.30A/C1-298[»]
2CLXX-ray1.80A1-298[»]
2DS1X-ray2.00A1-298[»]
2DUVX-ray2.20A1-298[»]
2EXMX-ray1.80A1-298[»]
2FVDX-ray1.85A1-298[»]
2G9XX-ray2.50A/C1-298[»]
2HICmodel-A1-298[»]
2I40X-ray2.80A/C1-298[»]
2IW6X-ray2.30A/C1-298[»]
2IW8X-ray2.30A/C1-298[»]
2IW9X-ray2.00A/C1-298[»]
2J9MX-ray2.50A1-298[»]
2JGZX-ray2.90A1-288[»]
2R3FX-ray1.50A1-298[»]
2R3GX-ray1.55A1-298[»]
2R3HX-ray1.50A1-298[»]
2R3IX-ray1.28A1-298[»]
2R3JX-ray1.65A1-298[»]
2R3KX-ray1.70A1-298[»]
2R3LX-ray1.65A1-298[»]
2R3MX-ray1.70A1-298[»]
2R3NX-ray1.63A1-298[»]
2R3OX-ray1.80A1-298[»]
2R3PX-ray1.66A1-298[»]
2R3QX-ray1.35A1-298[»]
2R3RX-ray1.47A1-298[»]
2R64X-ray2.30A1-298[»]
2UUEX-ray2.06A/C1-298[»]
2UZBX-ray2.70A/C1-298[»]
2UZDX-ray2.72A/C1-298[»]
2UZEX-ray2.40A/C1-298[»]
2UZLX-ray2.40A/C1-298[»]
2UZNX-ray2.30A1-298[»]
2UZOX-ray2.30A1-298[»]
2V0DX-ray2.20A1-298[»]
2V22X-ray2.60A/C1-298[»]
2VTAX-ray2.00A1-298[»]
2VTHX-ray1.90A1-298[»]
2VTIX-ray2.00A1-298[»]
2VTJX-ray2.20A1-298[»]
2VTLX-ray2.00A1-298[»]
2VTMX-ray2.25A1-298[»]
2VTNX-ray2.20A1-298[»]
2VTOX-ray2.19A1-298[»]
2VTPX-ray2.15A1-298[»]
2VTQX-ray1.90A1-298[»]
2VTRX-ray1.90A1-298[»]
2VTSX-ray1.90A1-298[»]
2VTTX-ray1.68A1-298[»]
2VU3X-ray1.85A1-298[»]
2VV9X-ray1.90A1-298[»]
2W05X-ray1.90A1-298[»]
2W06X-ray2.04A1-298[»]
2W17X-ray2.15A1-298[»]
2W1HX-ray2.15A1-298[»]
2WEVX-ray2.30A/C1-298[»]
2WFYX-ray2.53A/C1-298[»]
2WHAX-ray2.75A/C1-298[»]
2WHBX-ray2.90A/C1-298[»]
2WIHX-ray2.50A/C1-298[»]
2WIPX-ray2.80A/C1-298[»]
3BHTX-ray2.00A/C1-298[»]
3BHUX-ray2.30A/C1-298[»]
3BHVX-ray2.10A/C1-298[»]
3DDPX-ray2.70A/C1-298[»]
3DDQX-ray1.80A/C1-298[»]
3DOGX-ray2.70A/C1-298[»]
3EIDX-ray3.15A/C1-298[»]
3EJ1X-ray3.22A/C1-298[»]
3EOCX-ray3.20A/C1-298[»]
3EZRX-ray1.90A1-298[»]
3EZVX-ray1.99A1-298[»]
3F5XX-ray2.40A/C1-298[»]
3FZ1X-ray1.90A1-298[»]
3IG7X-ray1.80A1-298[»]
3IGGX-ray1.80A1-298[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-161N.
IntActP24941. 66 interactions.
STRINGP24941.

PTM databases

PhosphoSiteP24941.

Proteomic databases

PRIDEP24941.

Genome annotation databases

EnsemblENST00000266970; ENSP00000266970; ENSG00000123374; Homo sapiens. [Genome view]
GeneID1017.
KEGGhsa:1017.
UCSCuc001sit.2. human.

Organism-specific databases

CTD1017.
GeneCardsGC12P054646.
H-InvDBHIX0010710.
HGNCHGNC:1771. CDK2.
HPACAB013115.
MIM116953. gene.
PharmGKBPA101.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG755340.
HOVERGENP24941.
InParanoidP24941.
OMALDLKKYM.
OrthoDBEOG95QKZV.
PhylomeDBP24941.

Enzyme and pathway databases

BRENDA2.7.11.22. 247.
Pathway_Interaction_DBbard1pathway. 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.
ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP24941.
BgeeP24941.
CleanExHS_CDK2.
GenevestigatorP24941.
GermOnlineENSG00000123374. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP24941.
NextBio4273.
SOURCESearch...

Entry information

Entry nameCDK2_HUMAN
AccessionPrimary (citable) accession number: P24941
Secondary accession number(s): A8K7C6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: August 1, 1992
Last modified: February 9, 2010
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents