Cyclin-dependent kinase 2

"CDK2" redirects here. For the airport with the Transport Canada identifier CDK2, see Diavik Airport.

CDK2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes

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, 2C5V, 2C5X, 2C5Y, 2C68, 2C69, 2C6I, 2C6K, 2C6L, 2C6M, 2C6O, 2C6T, 2CCH, 2CCI, 2CJM, 2CLX, 2DS1, 2DUV, 2EXM, 2FVD, 2G9X, 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, 2WEV, 2WFY, 2WHB, 2WIH, 2WIP, 2WMA, 2WMB, 2WPA, 2WXV, 2X1N, 2XMY, 2XNB, 3BHT, 3BHU, 3BHV, 3DDP, 3DDQ, 3DOG, 3EID, 3EJ1, 3EOC, 3EZR, 3EZV, 3F5X, 3FZ1, 3IG7, 3IGG, 3LE6, 3LFN, 3LFQ, 3LFS, 3MY5, 3NS9, 3PJ8, 3PXF, 3PXQ, 3PXR, 3PXY, 3PXZ, 3PY0, 3PY1, 3QHR, 3QHW, 3QL8, 3QQF, 3QQG, 3QQH, 3QQJ, 3QQK, 3QQL, 3QRT, 3QRU, 3QTQ, 3QTR, 3QTS, 3QTU, 3QTW, 3QTX, 3QTZ, 3QU0, 3QWJ, 3QWK, 3QX2, 3QX4, 3QXO, 3QXP, 3QZF, 3QZG, 3QZH, 3QZI, 3R1Q, 3R1S, 3R1Y, 3R28, 3R6X, 3R71, 3R73, 3R7E, 3R7I, 3R7U, 3R7V, 3R7Y, 3R83, 3R8L, 3R8M, 3R8P, 3R8U, 3R8V, 3R8Z, 3R9D, 3R9H, 3R9N, 3R9O, 3RAH, 3RAI, 3RAK, 3RAL, 3RJC, 3RK5, 3RK7, 3RK9, 3RKB, 3RM6, 3RM7, 3RMF, 3RNI, 3ROY, 3RPO, 3RPR, 3RPV, 3RPY, 3RZB, 3S00, 3S0O, 3S1H, 3S2P, 3SQQ, 3SW4, 3SW7, 3TI1, 3TIY, 3TIZ, 3TNW, 3ULI, 3UNJ, 3UNK, 4ACM, 4BCK, 4BCM, 4BCN, 4BCO, 4BCP, 4BCQ, 4BGH, 4EK3, 4EK4, 4EK5, 4EK6, 4EK8, 4EOI, 4EOJ, 4EOK, 4EOL, 4EOM, 4EON, 4EOO, 4EOP, 4EOQ, 4EOR, 4EOS, 4ERW, 4EZ3, 4EZ7, 4FKG, 4FKI, 4FKJ, 4FKL, 4FKO, 4FKP, 4FKQ, 4FKR, 4FKS, 4FKT, 4FKU, 4FKV, 4FKW, 4FX3, 4GCJ, 4I3Z, 4II5, 3WBL, 4BZD, 4CFM, 4CFN, 4CFU, 4CFV, 4CFW, 4CFX, 4D1X, 4D1Z, 4KD1, 4LYN, 4NJ3, 4RJ3, 5A14, 5CYI, 5D1J, 5FP6, 5FP5, 5K4J, 5IF1, 5AND, 5ANG, 5ANI, 5ANK, 5ANE, 5IEX, 5IEV, 5ANJ, 5ANO, 5IEY

Identifiers

Aliases

CDK2, cyclin-dependent kinase 2, A630093N05Rik, CDKN2, p33(CDK2), cyclin dependent kinase 2

External IDs

MGI: 104772 HomoloGene: 74409 GeneCards: CDK2

Targeted by Drug

alvocidib, dinaciclib, seliciclib^[1]

Gene ontology
Molecular function	• transferase activity • protein kinase activity • nucleotide binding • cyclin-dependent protein serine/threonine kinase activity • histone kinase activity • protein complex binding • metal ion binding • protein binding • ATP binding • cyclin binding • kinase activity • protein serine/threonine kinase activity
Cellular component	• cytoplasm • cytosol • endosome • Cajal body • centrosome • cyclin-dependent protein kinase holoenzyme complex • intracellular membrane-bounded organelle • transcription factor complex • X chromosome • Y chromosome • microtubule organizing center • nucleoplasm • chromosome, telomeric region • cytoskeleton • condensed chromosome • nucleus
Biological process	• response to estradiol • response to cadmium ion • mitotic nuclear division • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • phosphorylation • centrosome duplication • G1/S transition of mitotic cell cycle • regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • response to electrical stimulus • regulation of cell cycle • cellular response to DNA damage stimulus • cell division • positive regulation of transcription, DNA-templated • DNA replication • potassium ion transport • protein phosphorylation • regulation of gene silencing • lens development in camera-type eye • meiotic cell cycle • G2/M transition of mitotic cell cycle • positive regulation of DNA-dependent DNA replication initiation • peptidyl-serine phosphorylation • animal organ regeneration • positive regulation of cell proliferation • mitotic G1 DNA damage checkpoint • cellular response to insulin stimulus • cell cycle • cellular response to nitric oxide • response to cAMP • Ras protein signal transduction • response to ethanol • centriole replication • meiotic nuclear division • response to toxic substance • response to drug • histone phosphorylation • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • regulation of signal transduction by p53 class mediator • DNA repair
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


1017


12566

Ensembl


ENSG00000123374


ENSMUSG00000025358

UniProt


P24941


P97377

RefSeq (mRNA)


NM_001290230 NM_001798 NM_052827


NM_016756 NM_183417

RefSeq (protein)


NP_001277159.1 NP_001789.2 NP_439892.2


NP_058036.1 NP_904326.1

Location (UCSC)

Chr 12: 55.97 – 55.97 Mb

Chr 10: 128.7 – 128.71 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Cyclin-dependent kinase 2, also known as cell division protein kinase 2, is an enzyme that in humans is encoded by the CDK2 gene.^[4]^[5]

Function

The protein encoded by this gene is a member of the cyclin-dependent kinase family of Ser/Thr protein kinases. This protein kinase is highly similar to the gene products of S. cerevisiae cdc28, and S. pombe cdc2, also known as Cdk1 in humans. It is a catalytic subunit of the cyclin-dependent kinase complex, whose activity is restricted to the G1-S phase of the cell cycle, and is essential for the G1/S transition. This protein associates with and is regulated by the regulatory subunits of the complex including cyclin E or A. Cyclin E binds G1 phase Cdk2, which is required for the transition from G1 to S phase while binding with Cyclin A is required to progress through the S phase. Its activity is also regulated by phosphorylation. Two alternatively spliced variants and multiple transcription initiation sites of this gene have been reported.^[5]

The role of this protein in G1-S transition has been recently questioned as cells lacking Cdk2 are reported to have no problem during this transition.^[6]

Inhibitors

Known CDK inhibitors are p21Cip1 (CDKN1A) and p27Kip1 (CDKN1B).^[7] Drugs that inhibit Cdk2 and arrest the cell cycle, such as GW8510 and the experimental cancer drug seliciclib, may reduce the sensitivity of the epithelium to many cell cycle-active antitumor agents and, therefore, represent a strategy for prevention of chemotherapy-induced alopecia.^[8]

Gene regulation

In melanocytic cell types, expression of the CDK2 gene is regulated by the Microphthalmia-associated transcription factor.^[9]^[10]

Interactions

Cyclin-dependent kinase 2 has been shown to interact with:

BRCA1,^[11]^[12]^[13]
CDK2AP1,^[14]
CDKN1B^[15]^[16]^[17]^[18]^[19]
CDKN3,^[20]^[21]^[22]
CEBPA,^[23]
Cyclin A1,^[24]^[25]^[26]^[27]
Cyclin E1,^[15]^[28]^[29]^[30]^[31]^[32]
Flap structure-specific endonuclease 1,^[33]
ORC1L,^[34]
P21,^[19]^[22]^[29]^[35]^[36]
PPM1B,^[37]
PPP2CA,^[37]
Retinoblastoma-like protein 1,^[28]^[38]
Retinoblastoma-like protein 2,^[28]^[39] and
SKP2.^[16]^[35]^[40]

Overview of signal transduction pathways involved in apoptosis.

References

↑ "Drugs that physically interact with Cyclin-dependent kinase 2 view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Tsai LH, Harlow E, Meyerson M (September 1991). "Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase". Nature. 353 (6340): 174–7. doi:10.1038/353174a0. PMID 1653904.
1 2 "Entrez Gene: CDK2 cyclin-dependent kinase 2".
1 2 Berthet C, Aleem E, Coppola V, Tessarollo L, Kaldis P (October 2003). "Cdk2 knockout mice are viable". Curr. Biol. 13 (20): 1775–85. doi:10.1016/j.cub.2003.09.024. PMID 14561402.
↑ Levkau B, Koyama H, Raines EW, Clurman BE, Herren B, Orth K, Roberts JM, Ross R (March 1998). "Cleavage of p21Cip1/Waf1 and p27Kip1 mediates apoptosis in endothelial cells through activation of Cdk2: role of a caspase cascade". Mol. Cell. 1 (4): 553–63. doi:10.1016/S1097-2765(00)80055-6. PMID 9660939.
↑ Davis ST, Benson BG, Bramson HN, Chapman DE, Dickerson SH, Dold KM, Eberwein DJ, Edelstein M, Frye SV, Gampe Jr RT, Griffin RJ, Harris PA, Hassell AM, Holmes WD, Hunter RN, Knick VB, Lackey K, Lovejoy B, Luzzio MJ, Murray D, Parker P, Rocque WJ, Shewchuk L, Veal JM, Walker DH, Kuyper LF (January 2001). "Prevention of chemotherapy-induced alopecia in rats by CDK inhibitors". Science. 291 (5501): 134–7. doi:10.1126/science.291.5501.134. PMID 11141566.
↑ Du J, Widlund HR, Horstmann MA, Ramaswamy S, Ross K, Huber WE, Nishimura EK, Golub TR, Fisher DE (2004). "Critical role of CDK2 for melanoma growth linked to its melanocyte-specific transcriptional regulation by MITF". Cancer Cell. 6 (6): 565–76. doi:10.1016/j.ccr.2004.10.014. PMID 15607961.
↑ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
↑ Chen Y, Farmer AA, Chen CF, Jones DC, Chen PL, Lee WH (July 1996). "BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed and phosphorylated in a cell cycle-dependent manner". Cancer Res. 56 (14): 3168–72. PMID 8764100.
↑ Ruffner H, Jiang W, Craig AG, Hunter T, Verma IM (July 1999). "BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site". Mol. Cell. Biol. 19 (7): 4843–54. PMC 84283. PMID 10373534.
↑ Wang H, Shao N, Ding QM, Cui J, Reddy ES, Rao VN (July 1997). "BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases". Oncogene. 15 (2): 143–57. doi:10.1038/sj.onc.1201252. PMID 9244350.
↑ Shintani S, Ohyama H, Zhang X, McBride J, Matsuo K, Tsuji T, Hu MG, Hu G, Kohno Y, Lerman M, Todd R, Wong DT (September 2000). "p12(DOC-1) is a novel cyclin-dependent kinase 2-associated protein". Mol. Cell. Biol. 20 (17): 6300–7. doi:10.1128/MCB.20.17.6300-6307.2000. PMC 86104. PMID 10938106.
1 2 Connor MK, Kotchetkov R, Cariou S, Resch A, Lupetti R, Beniston RG, Melchior F, Hengst L, Slingerland JM (January 2003). "CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis". Mol. Biol. Cell. 14 (1): 201–13. doi:10.1091/mbc.E02-06-0319. PMC 140238. PMID 12529437.
1 2 Rosner M, Hengstschläger M (November 2004). "Tuberin binds p27 and negatively regulates its interaction with the SCF component Skp2". J. Biol. Chem. 279 (47): 48707–15. doi:10.1074/jbc.M405528200. PMID 15355997.
↑ Youn CK, Cho HJ, Kim SH, Kim HB, Kim MH, Chang IY, Lee JS, Chung MH, Hahm KS, You HJ (February 2005). "Bcl-2 expression suppresses mismatch repair activity through inhibition of E2F transcriptional activity". Nat. Cell Biol. 7 (2): 137–47. doi:10.1038/ncb1215. PMID 15619620.
↑ Porter LA, Kong-Beltran M, Donoghue DJ (September 2003). "Spy1 interacts with p27Kip1 to allow G1/S progression". Mol. Biol. Cell. 14 (9): 3664–74. doi:10.1091/mbc.E02-12-0820. PMC 196558. PMID 12972555.
1 2 Law BK, Chytil A, Dumont N, Hamilton EG, Waltner-Law ME, Aakre ME, Covington C, Moses HL (December 2002). "Rapamycin potentiates transforming growth factor beta-induced growth arrest in nontransformed, oncogene-transformed, and human cancer cells". Mol. Cell. Biol. 22 (23): 8184–98. doi:10.1128/mcb.22.23.8184-8198.2002. PMC 134072. PMID 12417722.
↑ Yeh CT, Lu SC, Chao CH, Chao ML (May 2003). "Abolishment of the interaction between cyclin-dependent kinase 2 and Cdk-associated protein phosphatase by a truncated KAP mutant". Biochem. Biophys. Res. Commun. 305 (2): 311–4. doi:10.1016/s0006-291x(03)00757-5. PMID 12745075.
↑ Hannon GJ, Casso D, Beach D (March 1994). "KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases". Proc. Natl. Acad. Sci. U.S.A. 91 (5): 1731–5. doi:10.1073/pnas.91.5.1731. PMC 43237. PMID 8127873.
1 2 Harper JW, Adami GR, Wei N, Keyomarsi K, Elledge SJ (November 1993). "The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases". Cell. 75 (4): 805–16. doi:10.1016/0092-8674(93)90499-g. PMID 8242751.
↑ Wang H, Iakova P, Wilde M, Welm A, Goode T, Roesler WJ, Timchenko NA (October 2001). "C/EBPalpha arrests cell proliferation through direct inhibition of Cdk2 and Cdk4". Mol. Cell. 8 (4): 817–28. doi:10.1016/s1097-2765(01)00366-5. PMID 11684017.
↑ Sweeney C, Murphy M, Kubelka M, Ravnik SE, Hawkins CF, Wolgemuth DJ, Carrington M (January 1996). "A distinct cyclin A is expressed in germ cells in the mouse". Development. 122 (1): 53–64. PMID 8565853.
↑ Yang R, Morosetti R, Koeffler HP (March 1997). "Characterization of a second human cyclin A that is highly expressed in testis and in several leukemic cell lines". Cancer Res. 57 (5): 913–20. PMID 9041194.
↑ Müller-Tidow C, Wang W, Idos GE, Diederichs S, Yang R, Readhead C, Berdel WE, Serve H, Saville M, Watson R, Koeffler HP (April 2001). "Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2 phosphorylate B-myb at functionally important serine and threonine residues: tissue-specific regulation of B-myb function". Blood. 97 (7): 2091–7. doi:10.1182/blood.v97.7.2091. PMID 11264176.
↑ Brown NR, Noble ME, Endicott JA, Johnson LN (November 1999). "The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases". Nat. Cell Biol. 1 (7): 438–43. doi:10.1038/15674. PMID 10559988.
1 2 3 Shanahan F, Seghezzi W, Parry D, Mahony D, Lees E (February 1999). "Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest". Mol. Cell. Biol. 19 (2): 1460–9. doi:10.1128/mcb.19.2.1460. PMC 116074. PMID 9891079.
1 2 McKenzie PP, Danks MK, Kriwacki RW, Harris LC (July 2003). "P21Waf1/Cip1 dysfunction in neuroblastoma: a novel mechanism of attenuating G0-G1 cell cycle arrest". Cancer Res. 63 (13): 3840–4. PMID 12839982.
↑ Koff A, Giordano A, Desai D, Yamashita K, Harper JW, Elledge S, Nishimoto T, Morgan DO, Franza BR, Roberts JM (September 1992). "Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle". Science. 257 (5077): 1689–94. doi:10.1126/science.1388288. PMID 1388288.
↑ Mayer C, Zhao J, Yuan X, Grummt I (February 2004). "mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability". Genes Dev. 18 (4): 423–34. doi:10.1101/gad.285504. PMC 359396. PMID 15004009.
↑ Boudrez A, Beullens M, Groenen P, Van Eynde A, Vulsteke V, Jagiello I, Murray M, Krainer AR, Stalmans W, Bollen M (August 2000). "NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry". J. Biol. Chem. 275 (33): 25411–7. doi:10.1074/jbc.M001676200. PMID 10827081.
↑ Henneke G, Koundrioukoff S, Hübscher U (July 2003). "Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation". Oncogene. 22 (28): 4301–13. doi:10.1038/sj.onc.1206606. PMID 12853968.
↑ Méndez J, Zou-Yang XH, Kim SY, Hidaka M, Tansey WP, Stillman B (March 2002). "Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication". Mol. Cell. 9 (3): 481–91. doi:10.1016/s1097-2765(02)00467-7. PMID 11931757.
1 2 Yam CH, Ng RW, Siu WY, Lau AW, Poon RY (January 1999). "Regulation of cyclin A-Cdk2 by SCF component Skp1 and F-box protein Skp2". Mol. Cell. Biol. 19 (1): 635–45. PMC 83921. PMID 9858587.
↑ Ono T, Kitaura H, Ugai H, Murata T, Yokoyama KK, Iguchi-Ariga SM, Ariga H (October 2000). "TOK-1, a novel p21Cip1-binding protein that cooperatively enhances p21-dependent inhibitory activity toward CDK2 kinase". J. Biol. Chem. 275 (40): 31145–54. doi:10.1074/jbc.M003031200. PMID 10878006.
1 2 Cheng A, Kaldis P, Solomon MJ (November 2000). "Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms". J. Biol. Chem. 275 (44): 34744–9. doi:10.1074/jbc.M006210200. PMID 10934208.
↑ Leng X, Noble M, Adams PD, Qin J, Harper JW (April 2002). "Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4". Mol. Cell. Biol. 22 (7): 2242–54. doi:10.1128/mcb.22.7.2242-2254.2002. PMC 133692. PMID 11884610.
↑ Lacy S, Whyte P (May 1997). "Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes". Oncogene. 14 (20): 2395–406. doi:10.1038/sj.onc.1201085. PMID 9188854.
↑ Marti A, Wirbelauer C, Scheffner M, Krek W (May 1999). "Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation". Nat. Cell Biol. 1 (1): 14–9. doi:10.1038/8984. PMID 10559858.

External links

Cyclin-Dependent Kinase 2 at the US National Library of Medicine Medical Subject Headings (MeSH)
CDK2 human gene location in the UCSC Genome Browser.
CDK2 human gene details in the UCSC Genome Browser.

PDB gallery

1aq1: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR STAUROSPORINE

1b38: HUMAN CYCLIN-DEPENDENT KINASE 2

1b39: HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160

1buh: CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE COMPLEX WITH CELL CYCLE-REGULATORY PROTEIN CKSHS1

1ckp: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR PURVALANOL B

1di8: THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4-[3-HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE

1dm2: HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR HYMENIALDISINE

1e1v: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU2058

1e1x: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU6027

1e9h: THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE INHIBITOR INDIRUBIN-5-SULPHONATE BOUND

1f5q: CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN COMPLEXED TO HUMAN CYCLIN DEPENDENT KINASE 2

1fin: CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX

1fq1: CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) IN COMPLEX WITH PHOSPHO-CDK2

1fvt: THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH AN OXINDOLE INHIBITOR

1fvv: THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLE INHIBITOR

1g5s: CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH THE INHIBITOR H717

1gih: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR

1gii: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR

1gij: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR

1gy3: PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE SUBSTRATE

1gz8: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2-AMINO-6-(3'-METHYL-2'-OXO)BUTOXYPURINE

1h00: CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6-BIS ANILINO PYRIMIDINE CDK4 INHIBITOR

1h07: CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6-BIS ANILINO PYRIMIDINE CDK4 INHIBITOR

1h08: CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4-BIS ANILINO PYRIMIDINE CDK4 INHIBITOR

1h0v: HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE INHIBITOR 2-AMINO-6-[(R)-PYRROLIDINO-5'-YL]METHOXYPURINE

1h0w: HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE INHIBITOR 2-AMINO-6-[CYCLOHEX-3-ENYL]METHOXYPURINE

1h1p: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH THE INHIBITOR NU2058

1h1q: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH THE INHIBITOR NU6094

1h1r: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH THE INHIBITOR NU6086

1h1s: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH THE INHIBITOR NU6102

1h24: CDK2/CYCLIN A IN COMPLEX WITH A 9 RESIDUE RECRUITMENT PEPTIDE FROM E2F

1h25: CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM RETINOBLASTOMA-ASSOCIATED PROTEIN

1h26: CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM P53

1h27: CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM P27

1h28: CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM P107

1hck: HUMAN CYCLIN-DEPENDENT KINASE 2

1hcl: HUMAN CYCLIN-DEPENDENT KINASE 2

1jst: PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A

1jsu: P27(KIP1)/CYCLIN A/CDK2 COMPLEX

1jsv: The structure of cyclin-dependent kinase 2 (CDK2) in complex with 4-[(6-amino-4-pyrimidinyl)amino]benzenesulfonamide

1jvp: Crystal structure of human CDK2 (unphosphorylated) in complex with PKF049-365

1ke5: CDK2 complexed with N-methyl-4-{[(2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]amino}benzenesulfonamide

1ke6: CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{4-[2-(7-OXO-6,7-DIHYDRO-8H-[1,3]THIAZOLO[5,4-E]INDOL-8-YLIDENE)HYDRAZINO]PHENYL}METHANESULFONAMIDE

1ke7: CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-DIOXIDO-1,3-DIHYDRO-2-BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3-OXAZOL-5-YL)-1,3-DIHYDRO-2H-INDOL-2-ONE

1ke8: CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 4-{[(2-OXO-1,2-DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2-YL)BENZENESULFONAMIDE

1ke9: CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[4-({[AMINO(IMINO)METHYL]AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-DIHYDRO-1H-INDOLE

1ogu: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 2-ARYLAMINO-4-CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR

1oi9: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 6-CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR

1oiq: IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION

1oir: IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION

1oit: IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION

1oiu: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 6-CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR

1oiy: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 6-CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR

1okv: CYCLIN A BINDING GROOVE INHIBITOR H-ARG-ARG-LEU-ILE-PHE-NH2

1okw: CYCLIN A BINDING GROOVE INHIBITOR AC-ARG-ARG-LEU-ASN-(M-CL-PHE)-NH2

1ol1: CYCLIN A BINDING GROOVE INHIBITOR H-CIT-CIT-LEU-ILE-(P-F-PHE)-NH2

1ol2: CYCLIN A BINDING GROOVE INHIBITOR H-ARG-ARG-LEU-ASN-(P-F-PHE)-NH2

1p2a: The structure of cyclin dependent kinase 2 (CKD2) with a trisubstituted naphthostyril inhibitor

1p5e: The structure of phospho-CDK2/cyclin A in complex with the inhibitor 4,5,6,7-tetrabromobenzotriazole (TBS)

1pf8: Crystal Structure of Human Cyclin-Dependent Kinase 2 Complexed with a Nucleoside Inhibitor

1pkd: THE CRYSTAL STRUCTURE OF UCN-01 IN COMPLEX WITH PHOSPHO-CDK2/CYCLIN A

1pw2: APO STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2

1pxi: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 4-(2,5-Dichloro-thiophen-3-yl)-pyrimidin-2-ylamine

1pxj: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 4-(2,4-Dimethyl-thiazol-5-yl)-pyrimidin-2-ylamine

1pxk: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR N-[4-(2,4-Dimethyl-thiazol-5-yl)pyrimidin-2-yl]-N'-hydroxyiminoformamide

1pxl: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR [4-(2,4-Dimethyl-thiazol-5-yl)-pyrimidin-2-yl]-(4-trifluoromethyl-phenyl)-amine

1pxm: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 3-[4-(2,4-Dimethyl-thiazol-5-yl)-pyrimidin-2-ylamino]-phenol

1pxn: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 4-[4-(4-Methyl-2-methylamino-thiazol-5-yl)-pyrimidin-2-ylamino]-phenol

1pxo: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR [4-(2-Amino-4-methyl-thiazol-5-yl)-pyrimidin-2-yl]-(3-nitro-phenyl)-amine

1pxp: HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR N-[4-(2,4-Dimethyl-thiazol-5-yl)-pyrimidin-2-yl]-N',N'-dimethyl-benzene-1,4-diamine

1pye: Crystal structure of CDK2 with inhibitor

1qmz: PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX

1r78: CDK2 complex with a 4-alkynyl oxindole inhibitor

1urc: CYCLIN A BINDING GROOVE INHIBITOR ACE-ARG-LYS-LEU-PHE-GLY

1urw: CDK2 IN COMPLEX WITH AN IMIDAZO[1,2-B]PYRIDAZINE

1v1k: CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6-BIS ANILINO PYRIMIDINE CDK4 INHIBITOR

1vyw: STRUCTURE OF CDK2/CYCLIN A WITH PNU-292137

1vyz: STRUCTURE OF CDK2 COMPLEXED WITH PNU-181227

1w0x: CRYSTALS STRUCTURE OF HUMAN CDK2 IN COMPLEX WITH THE INHIBITOR OLOMOUCINE.

1w8c: CO-CRYSTAL STRUCTURE OF 6-CYCLOHEXYLMETHOXY-8-ISOPROPYL-9H-PURIN-2-YLAMINE AND MONOMERIC CDK2

1w98: THE STRUCTURAL BASIS OF CDK2 ACTIVATION BY CYCLIN E

1wcc: SCREENING FOR FRAGMENT BINDING BY X-RAY CRYSTALLOGRAPHY

1y8y: Crystal structure of human CDK2 complexed with a pyrazolo[1,5-a]pyrimidine inhibitor

1y91: Crystal structure of human CDK2 complexed with a pyrazolo[1,5-a]pyrimidine inhibitor

1ykr: Crystal structure of cdk2 with an aminoimidazo pyridine inhibitor

2a0c: Human CDK2 in complex with olomoucine II, a novel 2,6,9-trisubstituted purine cyclin-dependent kinase inhibitor

2a4l: Human cyclin-dependent kinase 2 in complex with roscovitine

2b52: Human cyclin dependent kinase 2 (CDK2) complexed with DPH-042562

2b53: Human cyclin dependent kinase 2 (CDK2) complexed with DIN-234325

2b54: Human cyclin dependent kinase 2 (CKD2)complexed with DIN-232305

2b55: Human cyclin dependent kinase 2 (cdk2) complexed with indenopyraxole DIN-101312

2bhe: HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE INHIBITOR 5-BROMO-INDIRUBINE

2bhh: HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE INHIBITOR 4-HYDROXYPIPERINDINESULFONYL-INDIRUBINE

2bkz: STRUCTURE OF CDK2-CYCLIN A WITH PHA-404611

2bpm: STRUCTURE OF CDK2-CYCLIN A WITH PHA-630529

2btr: STRUCTURE OF CDK2 COMPLEXED WITH PNU-198873

2bts: STRUCTURE OF CDK2 COMPLEXED WITH PNU-230032

2c4g: STRUCTURE OF CDK2-CYCLIN A WITH PHA-533514

2c5n: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN

2c5o: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN

2c5p:

2c5v: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN

2c5x: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN

2c5y: DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2 PROVIDES INSIGHTS FOR DRUG DESIGN

2c68: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR

2c69: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR

2c6i: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR

2c6k: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR

2c6l: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR

2c6m: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR

2c6o: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR

2c6t: CRYSTAL STRUCTURE OF THE HUMAN CDK2 COMPLEXED WITH THE TRIAZOLOPYRIMIDINE INHIBITOR

2cch: THE CRYSTAL STRUCTURE OF CDK2 CYCLIN A IN COMPLEX WITH A SUBSTRATE PEPTIDE DERIVED FROM CDC MODIFIED WITH A GAMMA-LINKED ATP ANALOGUE

2cci: CRYSTAL STRUCTURE OF PHOSPHO-CDK2 CYCLIN A IN COMPLEX WITH A PEPTIDE CONTAINING BOTH THE SUBSTRATE AND RECRUITMENT SITES OF CDC6

2cjm: MECHANISM OF CDK INHIBITION BY ACTIVE SITE PHOSPHORYLATION: CDK2 Y15P T160P IN COMPLEX WITH CYCLIN A STRUCTURE

2clx: 4-ARYLAZO-3,5-DIAMINO-1H-PYRAZOLE CDK INHIBITORS: SAR STUDY, CRYSTAL STRUCTURE IN COMPLEX WITH CDK2, SELECTIVITY, AND CELLULAR EFFECTS

2duv: Structure of CDK2 with a 3-hydroxychromones

2exm: Human CDK2 in complex with isopentenyladenine

2fvd: Cyclin Dependent Kinase 2 (CDK2) with diaminopyrimidine inhibitor

2g9x: Structure of Thr 160 phosphorylated CDK2/cyclin A in complex with the inhibitor NU6271

2i40: Cdk2/Cyclin A complexed with a thiophene carboxamide inhibitor

2iw6: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-CYCLIN A COMPLEXED WITH A BISANILINOPYRIMIDINE INHIBITOR

2iw8: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-CYCLIN A F82H-L83V-H84D MUTANT WITH AN O6-CYCLOHEXYLMETHYLGUANINE INHIBITOR

2iw9: STRUCTURE OF HUMAN THR160-PHOSPHO CDK2-CYCLIN A COMPLEXED WITH A BISANILINOPYRIMIDINE INHIBITOR

2jgz: CRYSTAL STRUCTURE OF PHOSPHO-CDK2 IN COMPLEX WITH CYCLIN B

2uue: REPLACE: A STRATEGY FOR ITERATIVE DESIGN OF CYCLIN BINDING GROOVE INHIBITORS

Cell cycle proteins

Cyclin

A (A1, A2)
B (B1, B2, B3)
D (D1, D2, D3)
E (E1, E2)

CDK

CDK inhibitor

INK4a/ARF (p14arf/p16, p15, p18, p19)
cip/kip (p21, p27, p57)

P53 p63 p73 family

Other

Phases and
checkpoints

Interphase	G₁ phase S phase G₂ phase

M phase	Mitosis (Preprophase Prophase Prometaphase Metaphase Anaphase Telophase) Cytokinesis

Cell cycle checkpoints	Restriction point Spindle checkpoint Postreplication checkpoint

Other cellular phases	Apoptosis G₀ phase Meiosis

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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