[1]	SEQUENCE FROM NUCLEIC ACID. MEDLINE=91330891; 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]	SEQUENCE FROM NUCLEIC ACID. MEDLINE=91367262; 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]	SEQUENCE FROM NUCLEIC ACID. MEDLINE=92020980; 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]	PHOSPHORYLATION SITES. MEDLINE=93010995; 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).
[5]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). MEDLINE=93288132; 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).
[6]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CYCLIN A. MEDLINE=95356811; 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).
[7]	X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF COMPLEX WITH L868276. MEDLINE=96181476; PubMed=8610110; [NCBI, ExPASy, EBI, Israel, Japan] de Azevedo W.F. Jr., Muleer-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).
[8]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CG2A AND KIP1. MEDLINE=96300318; 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).
[9]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH CG2A. MEDLINE=96313126; 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).
[10]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). MEDLINE=97075215; 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).
[11]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). MEDLINE=97475219; 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).
[12]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITG CKS1. MEDLINE=96182647; 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).
[13]	X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). MEDLINE=98342369; 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).

Comments

FUNCTION: PROBABLY INVOLVED IN THE CONTROL OF THE CELL CYCLE. INTERACTS WITH CYCLINS A, D, OR E. ACTIVITY OF CDK2 IS MAXIMAL DURING S PHASE AND G2.
ENZYME REGULATION: PHOSPHORYLATION AT THR-14 OR TYR-15 INACTIVATES THE ENZYME, WHILE PHOSPHORYLATION AT THR-160 ACTIVATES IT.
SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CDC2/CDKX SUBFAMILY.

Copyright

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Cross-references

EMBL

X61622; CAA43807.1; -.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X62071; CAA43985.1; -.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M68520; AAA35667.1; -.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41227; A41227.
S16520; S16520.
S17873; S17873.

PDB

1FIN; 27-JAN-97.	[ExPASy / RCSB]
1HCK; 07-DEC-96.	[ExPASy / RCSB]
1HCL; 07-DEC-96.	[ExPASy / RCSB]
1AQ1; 12-NOV-97.	[ExPASy / RCSB]
1JST; 11-JAN-97.	[ExPASy / RCSB]
1JSU; 29-JUL-97.	[ExPASy / RCSB]
1BUH; 09-SEP-98.	[ExPASy / RCSB]
1B38; 23-DEC-98.	[ExPASy / RCSB]
1B39; 23-DEC-98.	[ExPASy / RCSB]
1CKP; 13-JAN-99.	[ExPASy / RCSB]

116953 [NCBI / EBI].

IPR000719; Euk_pkinase.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

PS00107; PROTEIN_KINASE_ATP; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS50011; PROTEIN_KINASE_DOM; 1.

ProDom

[Domain structure / List of seq. sharing at least 1 domain].

GET REGION ON 2D PAGE.

Keywords

Transferase; Serine/threonine-protein kinase; ATP-binding; Cell cycle; Cell division; Mitosis; Phosphorylation; 3D-structure.

Features

`Key`	`From To`	`Length`	`Description`
`DOMAIN`	`4 286`	`283`	`PROTEIN KINASE.`
`NP_BIND`	`10 18`	`9`	`ATP (BY SIMILARITY).`
`BINDING`	`33 33`		`ATP (BY SIMILARITY).`
`ACT_SITE`	`127 127`		`BY SIMILARITY.`
`MOD_RES`	`14 14`		`PHOSPHORYLATION.`
`MOD_RES`	`15 15`		`PHOSPHORYLATION.`
`MOD_RES`	`160 160`		`PHOSPHORYLATION (BY CAK).`
`MUTAGEN`	`14 14`		`T->A: INCREASE ACTIVITY 2 FOLD.`
`MUTAGEN`	`15 15`		`Y->F: INCREASE ACTIVITY 2 FOLD.`
`MUTAGEN`	`160 160`		`T->A: ABOLISHES ACTIVITY.`

Feature table viewer

Sequence information

Length: 298 AA

Molecular weight: 33929 Da

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

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