Reviewed, UniProtKB/Swiss-Prot P24941 (CDK2_HUMAN)

Names and origin

Protein names

Recommended name:
    Cell division protein kinase 2
    EC=2.7.11.22
Alternative name(s):
    p33 protein kinase

Gene names

Name:

CDK2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from Experiment. Source: Reactome G2/M transition of mitotic cell cycle Ref.2 Traceable author statement. Source: ProtInc Ras protein signal transduction Inferred from expression pattern. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cell proliferation Traceable author statement. Source: ProtInc regulation of DNA replication Traceable author statement. Source: ProtInc traversing start control point of mitotic cell cycle Traceable author statement. Source: ProtInc
Cellular component	cyclin-dependent protein kinase holoenzyme complex Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cyclin-dependent protein kinase activity Ref.2 Inferred from Experiment. Source: Reactome identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-375096,EBI-375096
CASP4	P49662	1	EBI-375096,EBI-1057327
CCNB2	O95067	1	EBI-375096,EBI-375024
CCNE1	P24864	4	EBI-375096,EBI-519526
CCNE2	O96020	5	EBI-375096,EBI-375033
CDKN1A	P38936	5	EBI-375096,EBI-375077
CDKN1B	P46527	6	EBI-375096,EBI-519280
CDKN3	Q16667	1	EBI-375096,EBI-1031527
EPB41	P11171	1	EBI-375096,EBI-1050906
FAM113A	Q9H1Q7	1	EBI-375096,EBI-748452
FBL	P22087	1	EBI-375096,EBI-358318
MCM3	P25205	1	EBI-375096,EBI-355153
MDM20	Q14CX7	1	EBI-375096,EBI-1048503
NEDD8	Q15843	1	EBI-375096,EBI-716247
OGT	O15294	1	EBI-375096,EBI-539828
ORC2L	Q13416	1	EBI-375096,EBI-374957
PEBP1	P30086	1	EBI-375096,EBI-716384
PFTK2	Q96Q40	1	EBI-375096,EBI-1051975
PPP1CA	P62136	1	EBI-375096,EBI-357253
PPP1CC	P36873-1	1	EBI-375096,EBI-356289
PTP4A3	O75365	1	EBI-375096,EBI-1043866
RADIL	Q96JH8	1	EBI-375096,EBI-744267
RB1	P06400	1	EBI-375096,EBI-491274
SORT1	Q99523	1	EBI-375096,EBI-1057058
TSC22D1	Q15714	1	EBI-375096,EBI-712609
UBE2M	P61081	1	EBI-375096,EBI-1041660
UHRF2	Q96PU4	4	EBI-375096,EBI-625304
VHL	P40337	1	EBI-375096,EBI-301246
WDR8	Q9P2S5	1	EBI-375096,EBI-1054904

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_0000085769

Regions

Domain

4 – 286

283

Protein kinase

Nucleotide binding

10 – 18

9

ATP

Nucleotide binding

81 – 83

3

ATP

Nucleotide binding

129 – 132

4

ATP

Sites

Active site

127

1

Proton acceptor

Binding site

33

1

ATP

Binding site

86

1

ATP

Binding site

145

1

ATP

Amino acid modifications

Modified residue

6

1

N6-acetyllysine Ref.25

Modified residue

14

1

Phosphothreonine Ref.9 Ref.16 Ref.19

Modified residue

15

1

Phosphotyrosine; by WEE1 Ref.9 Ref.19 Ref.18 Ref.20 Ref.22 Ref.24

Modified residue

19

1

Phosphotyrosine Ref.19 Ref.18

Modified residue

46

1

Phosphoserine Ref.20

Modified residue

158

1

Phosphothreonine

Modified residue

159

1

Phosphotyrosine

Modified residue

160

1

Phosphothreonine; by CAK and CCRK Ref.9 Ref.19 Ref.24 Ref.15

Natural variations

Natural variant

15

1

Y → S: dbSNP rs3087335.

VAR_016157

Natural variant

18

1

V → L: dbSNP rs11554376.

VAR_053927

Natural variant

45

1

P → L in a glioblastoma multiforme sample; somatic mutation. Ref.36

VAR_041972

Natural variant

290

1

T → S: dbSNP rs2069413. Ref.36 Ref.5

VAR_019988

Experimental info

Mutagenesis

14

1

T → A: 2-fold increase in activity. Ref.9

Mutagenesis

15

1

Y → F: 2-fold increase in activity. Ref.9

Mutagenesis

160

1

T → A: Abolishes activity. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

298

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Beta strand

14 – 23

10

Turn

24 – 26

3

Beta strand

29 – 35

7

Helix

46 – 55

10

Beta strand

66 – 72

7

Beta strand

75 – 81

7

Beta strand

84 – 86

3

Helix

87 – 93

7

Turn

94 – 97

4

Helix

101 – 120

20

Helix

130 – 132

3

Beta strand

133 – 135

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	P24941-1 [UniParc]. Last modified August 1, 1992. Version 2. Checksum: F90A0F4E70910B51	FASTA	298	33,930
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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

NIEHS-SNPs

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.

IPI

IPI00031681.

PIR

A41227.

RefSeq

NP_001789.2.
NP_439892.2.

UniGene

Hs.19192
Hs.689624

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AQ1	X-ray	2.00	A	1-298	[»]
1B38	X-ray	2.00	A	1-298	[»]
1B39	X-ray	2.10	A	1-298	[»]
1BUH	X-ray	2.60	A	1-298	[»]
1CKP	X-ray	2.05	A	1-298	[»]
1DI8	X-ray	2.20	A	1-298	[»]
1DM2	X-ray	2.10	A	1-298	[»]
1E1V	X-ray	1.95	A	1-298	[»]
1E1X	X-ray	1.85	A	1-298	[»]
1E9H	X-ray	2.50	A/C	1-296	[»]
1F5Q	X-ray	2.50	A/C	1-298	[»]
1FIN	X-ray	2.30	A/C	1-298	[»]
1FQ1	X-ray	3.00	B	1-298	[»]
1FVT	X-ray	2.20	A	1-298	[»]
1FVV	X-ray	2.80	A/C	1-298	[»]
1G5S	X-ray	2.61	A	1-298	[»]
1GIH	X-ray	2.80	A	1-298	[»]
1GII	X-ray	2.00	A	1-298	[»]
1GIJ	X-ray	2.20	A	1-298	[»]
1GY3	X-ray	2.70	A/C	1-296	[»]
1GZ8	X-ray	1.30	A	1-298	[»]
1H00	X-ray	1.60	A	1-298	[»]
1H01	X-ray	1.79	A	1-298	[»]
1H07	X-ray	1.85	A	1-298	[»]
1H08	X-ray	1.80	A	1-298	[»]
1H0V	X-ray	1.90	A	1-298	[»]
1H0W	X-ray	2.10	A	1-298	[»]
1H1P	X-ray	2.10	A/C	1-298	[»]
1H1Q	X-ray	2.50	A/C	1-298	[»]
1H1R	X-ray	2.00	A/C	1-298	[»]
1H1S	X-ray	2.00	A/C	1-298	[»]
1H24	X-ray	2.50	A/C	1-298	[»]
1H25	X-ray	2.50	A/C	1-298	[»]
1H26	X-ray	2.24	A/C	1-298	[»]
1H27	X-ray	2.20	A/C	1-298	[»]
1H28	X-ray	2.80	A/C	1-298	[»]
1HCK	X-ray	1.90	A	1-298	[»]
1HCL	X-ray	1.80	A	1-298	[»]
1JST	X-ray	2.60	A/C	1-298	[»]
1JSU	X-ray	2.30	A	1-298	[»]
1JSV	X-ray	1.96	A	1-298	[»]
1JVP	X-ray	1.53	P	1-298	[»]
1KE5	X-ray	2.20	A	1-298	[»]
1KE6	X-ray	2.00	A	1-298	[»]
1KE7	X-ray	2.00	A	1-298	[»]
1KE8	X-ray	2.00	A	1-298	[»]
1KE9	X-ray	2.00	A	1-298	[»]
1OGU	X-ray	2.60	A/C	1-298	[»]
1OI9	X-ray	2.10	A/C	1-298	[»]
1OIQ	X-ray	2.31	A	1-298	[»]
1OIR	X-ray	1.91	A	1-298	[»]
1OIT	X-ray	1.60	A	1-298	[»]
1OIU	X-ray	2.00	A/C	1-298	[»]
1OIY	X-ray	2.40	A/C	1-298	[»]
1OKV	X-ray	2.40	A/C	1-298	[»]
1OKW	X-ray	2.50	A/C	1-298	[»]
1OL1	X-ray	2.90	A/C	1-298	[»]
1OL2	X-ray	2.60	A/C	1-298	[»]
1P2A	X-ray	2.50	A	1-298	[»]
1P5E	X-ray	2.22	A/C	1-298	[»]
1PF8	X-ray	2.51	A	1-298	[»]
1PKD	X-ray	2.30	A/C	1-296	[»]
1PW2	X-ray	1.95	A	1-298	[»]
1PXI	X-ray	1.95	A	1-298	[»]
1PXJ	X-ray	2.30	A	1-298	[»]
1PXK	X-ray	2.80	A	1-298	[»]
1PXL	X-ray	2.50	A	1-298	[»]
1PXM	X-ray	2.53	A	1-298	[»]
1PXN	X-ray	2.50	A	1-298	[»]
1PXO	X-ray	1.96	A	1-298	[»]
1PXP	X-ray	2.30	A	1-298	[»]
1PYE	X-ray	2.00	A	1-298	[»]
1QMZ	X-ray	2.20	A/C	1-298	[»]
1R78	X-ray	2.00	A	1-298	[»]
1URC	X-ray	2.60	A/C	1-298	[»]
1URW	X-ray	1.60	A	1-298	[»]
1V1K	X-ray	2.31	A	1-298	[»]
1VYW	X-ray	2.30	A/C	1-298	[»]
1VYZ	X-ray	2.21	A	1-298	[»]
1W0X	X-ray	2.20	C	1-298	[»]
1W8C	X-ray	2.05	A	1-298	[»]
1W98	X-ray	2.15	A	1-297	[»]
1WCC	X-ray	2.20	A	1-298	[»]
1Y8Y	X-ray	2.00	A	1-298	[»]
1Y91	X-ray	2.15	A	1-298	[»]
1YKR	X-ray	1.80	A	1-298	[»]
2A0C	X-ray	1.95	X	1-298	[»]
2A4L	X-ray	2.40	A	1-298	[»]
2B52	X-ray	1.88	A	1-298	[»]
2B53	X-ray	2.00	A	1-298	[»]
2B54	X-ray	1.85	A	1-298	[»]
2B55	X-ray	1.85	A	1-298	[»]
2BHE	X-ray	1.90	A	1-298	[»]
2BHH	X-ray	2.60	A	1-298	[»]
2BKZ	X-ray	2.60	A/C	1-298	[»]
2BPM	X-ray	2.40	A/C	1-298	[»]
2BTR	X-ray	1.85	A	1-298	[»]
2BTS	X-ray	1.99	A	1-298	[»]
2C4G	X-ray	2.70	A/C	1-298	[»]
2C5N	X-ray	2.10	A/C	1-298	[»]
2C5O	X-ray	2.10	A/C	1-298	[»]
2C5V	X-ray	2.90	A/C	1-298	[»]
2C5X	X-ray	2.90	A/C	1-298	[»]
2C5Y	X-ray	2.25	A	1-298	[»]
2C68	X-ray	1.95	A	1-298	[»]
2C69	X-ray	2.10	A	1-298	[»]
2C6I	X-ray	1.80	A	1-298	[»]
2C6K	X-ray	1.90	A	1-298	[»]
2C6L	X-ray	2.30	A	1-298	[»]
2C6M	X-ray	1.90	A	1-298	[»]
2C6O	X-ray	2.10	A	1-298	[»]
2C6T	X-ray	2.61	A/C	1-298	[»]
2CCH	X-ray	1.70	A/C	1-298	[»]
2CCI	X-ray	2.70	A/C	1-298	[»]
2CJM	X-ray	2.30	A/C	1-298	[»]
2CLX	X-ray	1.80	A	1-298	[»]
2DS1	X-ray	2.00	A	1-298	[»]
2DUV	X-ray	2.20	A	1-298	[»]
2EXM	X-ray	1.80	A	1-298	[»]
2FVD	X-ray	1.85	A	1-298	[»]
2G9X	X-ray	2.50	A/C	1-298	[»]
2HIC	model	-	A	1-298	[»]
2I40	X-ray	2.80	A/C	1-298	[»]
2IW6	X-ray	2.30	A/C	1-298	[»]
2IW8	X-ray	2.30	A/C	1-298	[»]
2IW9	X-ray	2.00	A/C	1-298	[»]
2J9M	X-ray	2.50	A	1-298	[»]
2JGZ	X-ray	2.90	A	1-288	[»]
2R3F	X-ray	1.50	A	1-298	[»]
2R3G	X-ray	1.55	A	1-298	[»]
2R3H	X-ray	1.50	A	1-298	[»]
2R3I	X-ray	1.28	A	1-298	[»]
2R3J	X-ray	1.65	A	1-298	[»]
2R3K	X-ray	1.70	A	1-298	[»]
2R3L	X-ray	1.65	A	1-298	[»]
2R3M	X-ray	1.70	A	1-298	[»]
2R3N	X-ray	1.63	A	1-298	[»]
2R3O	X-ray	1.80	A	1-298	[»]
2R3P	X-ray	1.66	A	1-298	[»]
2R3Q	X-ray	1.35	A	1-298	[»]
2R3R	X-ray	1.47	A	1-298	[»]
2R64	X-ray	2.30	A	1-298	[»]
2UUE	X-ray	2.06	A/C	1-298	[»]
2UZB	X-ray	2.70	A/C	1-298	[»]
2UZD	X-ray	2.72	A/C	1-298	[»]
2UZE	X-ray	2.40	A/C	1-298	[»]
2UZL	X-ray	2.40	A/C	1-298	[»]
2UZN	X-ray	2.30	A	1-298	[»]
2UZO	X-ray	2.30	A	1-298	[»]
2V0D	X-ray	2.20	A	1-298	[»]
2V22	X-ray	2.60	A/C	1-298	[»]
2VTA	X-ray	2.00	A	1-298	[»]
2VTH	X-ray	1.90	A	1-298	[»]
2VTI	X-ray	2.00	A	1-298	[»]
2VTJ	X-ray	2.20	A	1-298	[»]
2VTL	X-ray	2.00	A	1-298	[»]
2VTM	X-ray	2.25	A	1-298	[»]
2VTN	X-ray	2.20	A	1-298	[»]
2VTO	X-ray	2.19	A	1-298	[»]
2VTP	X-ray	2.15	A	1-298	[»]
2VTQ	X-ray	1.90	A	1-298	[»]
2VTR	X-ray	1.90	A	1-298	[»]
2VTS	X-ray	1.90	A	1-298	[»]
2VTT	X-ray	1.68	A	1-298	[»]
2VU3	X-ray	1.85	A	1-298	[»]
2VV9	X-ray	1.90	A	1-298	[»]
2W05	X-ray	1.90	A	1-298	[»]
2W06	X-ray	2.04	A	1-298	[»]
2W17	X-ray	2.15	A	1-298	[»]
2W1H	X-ray	2.15	A	1-298	[»]
2WEV	X-ray	2.30	A/C	1-298	[»]
2WFY	X-ray	2.53	A/C	1-298	[»]
2WHA	X-ray	2.75	A/C	1-298	[»]
2WHB	X-ray	2.90	A/C	1-298	[»]
2WIH	X-ray	2.50	A/C	1-298	[»]
2WIP	X-ray	2.80	A/C	1-298	[»]
3BHT	X-ray	2.00	A/C	1-298	[»]
3BHU	X-ray	2.30	A/C	1-298	[»]
3BHV	X-ray	2.10	A/C	1-298	[»]
3DDP	X-ray	2.70	A/C	1-298	[»]
3DDQ	X-ray	1.80	A/C	1-298	[»]
3DOG	X-ray	2.70	A/C	1-298	[»]
3EID	X-ray	3.15	A/C	1-298	[»]
3EJ1	X-ray	3.22	A/C	1-298	[»]
3EOC	X-ray	3.20	A/C	1-298	[»]
3EZR	X-ray	1.90	A	1-298	[»]
3EZV	X-ray	1.99	A	1-298	[»]
3F5X	X-ray	2.40	A/C	1-298	[»]
3FZ1	X-ray	1.90	A	1-298	[»]
3IG7	X-ray	1.80	A	1-298	[»]
3IGG	X-ray	1.80	A	1-298	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-161N.

IntAct

P24941. 66 interactions.

STRING

P24941.

PTM databases

PhosphoSite

P24941.

Proteomic databases

PRIDE

P24941.

Genome annotation databases

Ensembl

ENST00000266970; ENSP00000266970; ENSG00000123374; Homo sapiens. [Genome view]

GeneID

1017.

KEGG

hsa:1017.

UCSC

uc001sit.2. human.

Organism-specific databases

CTD

1017.

GeneCards

GC12P054646.

H-InvDB

HIX0010710.

HGNC

HGNC:1771. CDK2.

HPA

CAB013115.

MIM

116953. gene.

PharmGKB

PA101.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG755340.

HOVERGEN

P24941.

InParanoid

P24941.

OMA

LDLKKYM.

OrthoDB

EOG95QKZV.

PhylomeDB

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.

Gene expression databases

ArrayExpress

P24941.

Bgee

P24941.

CleanEx

HS_CDK2.

Genevestigator

P24941.

GermOnline

ENSG00000123374. Homo sapiens.

Family and domain databases

InterPro

IPR011009. 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]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

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...

Other Resources

BindingDB

P24941.

NextBio

4273.

SOURCE

Search...

Entry information

Entry name

CDK2_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.