ID CDK2_HUMAN Reviewed; 298 AA. AC P24941; A8K7C6; O75100; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 2. DT 27-MAR-2024, entry version 267. DE RecName: Full=Cyclin-dependent kinase 2; DE EC=2.7.11.22 {ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:28666995, ECO:0000269|PubMed:9030781}; DE AltName: Full=Cell division protein kinase 2; DE AltName: Full=p33 protein kinase; GN Name=CDK2; Synonyms=CDKN2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1714386; DOI=10.1002/j.1460-2075.1991.tb07808.x; RA Elledge S.J., Spottswood M.R.; RT "A new human p34 protein kinase, CDK2, identified by complementation of a RT cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus Eg1."; RL EMBO J. 10:2653-2659(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1653904; DOI=10.1038/353174a0; RA Tsai L.-H., Harlow E., Meyerson M.; RT "Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus RT E1A-associated p33 kinase."; RL Nature 353:174-177(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1717994; DOI=10.1073/pnas.88.20.9006; RA Ninomiya-Tsuji J., Nomoto S., Yasuda H., Reed S.I., Matsumoto K.; RT "Cloning of a human cDNA encoding a CDC2-related kinase by complementation RT of a budding yeast cdc28 mutation."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9006-9010(1991). RN [4] RP NUCLEOTIDE SEQUENCE (ISOFORM 2). RA Nishikawa T., Ohta T., Fukuda M., Ogata H., Okamoto K., Isohashi F., RA Arima K., Yamaguchi S.; RT "Sequence of deletion type cdk2 variant in human breast cancer."; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-290. RG NIEHS SNPs program; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT THR-14; TYR-15 RP AND THR-160, AND MUTAGENESIS OF THR-14; TYR-15 AND THR-160. RX PubMed=1396589; DOI=10.1002/j.1460-2075.1992.tb05493.x; RA Gu Y., Rosenblatt J., O'Morgan D.O.; RT "Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and RT Tyr15."; RL EMBO J. 11:3995-4005(1992). RN [12] RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION BY ROSCOVITINE AND OLOMOUCINE. RX PubMed=9030781; DOI=10.1111/j.1432-1033.1997.t01-2-00527.x; RA Meijer L., Borgne A., Mulner O., Chong J.P.J., Blow J.J., Inagaki N., RA Inagaki M., Delcros J.-G., Moulinoux J.-P.; RT "Biochemical and cellular effects of roscovitine, a potent and selective RT inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5."; RL Eur. J. Biochem. 243:527-536(1997). RN [13] RP FUNCTION AS RB1 KINASE, AND INTERACTION WITH CYCLIN E. RX PubMed=10499802; DOI=10.1016/s0092-8674(00)81519-6; RA Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C.; RT "Cdk phosphorylation triggers sequential intramolecular interactions that RT progressively block Rb functions as cells move through G1."; RL Cell 98:859-869(1999). RN [14] RP FUNCTION AS NPM1 KINASE. RX PubMed=11051553; DOI=10.1016/s0092-8674(00)00093-3; RA Okuda M., Horn H.F., Tarapore P., Tokuyama Y., Smulian A.G., Chan P.K., RA Knudsen E.S., Hofmann I.A., Snyder J.D., Bove K.E., Fukasawa K.; RT "Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome RT duplication."; RL Cell 103:127-140(2000). RN [15] RP FUNCTION AS NPAT KINASE. RX PubMed=10995386; DOI=10.1101/gad.827700; RA Zhao J., Kennedy B.K., Lawrence B.D., Barbie D.A., Matera A.G., RA Fletcher J.A., Harlow E.; RT "NPAT links cyclin E-Cdk2 to the regulation of replication-dependent RT histone gene transcription."; RL Genes Dev. 14:2283-2297(2000). RN [16] RP FUNCTION AS NPAT KINASE, AND SUBCELLULAR LOCATION. RX PubMed=10995387; DOI=10.1101/gad.829500; RA Ma T., Van Tine B.A., Wei Y., Garrett M.D., Nelson D., Adams P.D., Wang J., RA Qin J., Chow L.T., Harper J.W.; RT "Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in RT Cajal bodies promotes histone gene transcription."; RL Genes Dev. 14:2298-2313(2000). RN [17] RP FUNCTION AS P53/TP53 KINASE, AND INTERACTION WITH CYCLIN A AND CYCLIN B1. RX PubMed=10884347; DOI=10.1006/jmbi.2000.3830; RA Luciani M.G., Hutchins J.R.A., Zheleva D., Hupp T.R.; RT "The C-terminal regulatory domain of p53 contains a functional docking site RT for cyclin A."; RL J. Mol. Biol. 300:503-518(2000). RN [18] RP FUNCTION AS CDK7 KINASE, AND PHOSPHORYLATION BY CDK7. RX PubMed=11113184; DOI=10.1128/mcb.21.1.88-99.2001; RA Garrett S., Barton W.A., Knights R., Jin P., Morgan D.O., Fisher R.P.; RT "Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by RT substrate specificity determinants outside the T loop."; RL Mol. Cell. Biol. 21:88-99(2001). RN [19] RP INTERACTION WITH CCNB3. RX PubMed=12185076; DOI=10.1074/jbc.m203951200; RA Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S., Wang X.-Y., RA Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.; RT "Characterization and expression of mammalian cyclin b3, a prepachytene RT meiotic cyclin."; RL J. Biol. Chem. 277:41960-41969(2002). RN [20] RP INTERACTION WITH SPDYA. RX PubMed=11980914; DOI=10.1083/jcb.200109045; RA Porter L.A., Dellinger R.W., Tynan J.A., Barnes E.A., Kong M., RA Lenormand J.-L., Donoghue D.J.; RT "Human Speedy: a novel cell cycle regulator that enhances proliferation RT through activation of Cdk2."; RL J. Cell Biol. 157:357-366(2002). RN [21] RP INTERACTION WITH SPDYA. RX PubMed=12839962; RA Barnes E.A., Porter L.A., Lenormand J.-L., Dellinger R.W., Donoghue D.J.; RT "Human Spy1 promotes survival of mammalian cells following DNA damage."; RL Cancer Res. 63:3701-3707(2003). RN [22] RP FUNCTION. RX PubMed=12944431; DOI=10.1242/dev.00731; RA Terret M.E., Lefebvre C., Djiane A., Rassinier P., Moreau J., Maro B., RA Verlhac M.H.; RT "DOC1R: a MAP kinase substrate that control microtubule organization of RT metaphase II mouse oocytes."; RL Development 130:5169-5177(2003). RN [23] RP INTERACTION WITH SPDYA, AND IDENTIFICATION IN A COMPLEX WITH CDKN1B AND RP SPDYA. RX PubMed=12972555; DOI=10.1091/mbc.e02-12-0820; RA Porter L.A., Kong-Beltran M., Donoghue D.J.; RT "Spy1 interacts with p27Kip1 to allow G1/S progression."; RL Mol. Biol. Cell 14:3664-3674(2003). RN [24] RP INTERACTION WITH UHRF2, AND IDENTIFICATION IN A COMPLEX WITH UHRF2 AND RP CCNE1. RX PubMed=15178429; DOI=10.1016/j.bbrc.2004.04.190; RA Li Y., Mori T., Hata H., Homma Y., Kochi H.; RT "NIRF induces G1 arrest and associates with Cdk2."; RL Biochem. Biophys. Res. Commun. 319:464-468(2004). RN [25] RP INTERACTION WITH CEBPA. RX PubMed=15107404; DOI=10.1101/gad.1183304; RA Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.; RT "Liver tumors escape negative control of proliferation via PI3K/Akt- RT mediated block of C/EBP alpha growth inhibitory activity."; RL Genes Dev. 18:912-925(2004). RN [26] RP PHOSPHORYLATION AT THR-160. RX PubMed=14597612; DOI=10.1074/jbc.m309995200; RA Liu Y., Wu C., Galaktionov K.; RT "p42, a novel cyclin-dependent kinase-activating kinase in mammalian RT cells."; RL J. Biol. Chem. 279:4507-4514(2004). RN [27] RP INTERACTION WITH SPDYA AND SPDYC. RX PubMed=15611625; DOI=10.4161/cc.4.1.1347; RA Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.; RT "Identification and comparative analysis of multiple mammalian Speedy/Ringo RT proteins."; RL Cell Cycle 4:155-165(2005). RN [28] RP FUNCTION AS BRCA2 KINASE. RX PubMed=15800615; DOI=10.1038/nature03404; RA Esashi F., Christ N., Gannon J., Liu Y., Hunt T., Jasin M., West S.C.; RT "CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for RT recombinational repair."; RL Nature 434:598-604(2005). RN [29] RP PHOSPHORYLATION BY CAK, MUTAGENESIS OF LYS-9; 88-LYS-LYS-89 AND LEU-166, RP AND INTERACTION WITH CDK7. RX PubMed=17373709; DOI=10.1002/prot.21370; RA Lolli G., Johnson L.N.; RT "Recognition of Cdk2 by Cdk7."; RL Proteins 67:1048-1059(2007). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [31] RP FUNCTION IN MITOSE REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=18372919; DOI=10.1038/onc.2008.74; RA De Boer L., Oakes V., Beamish H., Giles N., Stevens F., RA Somodevilla-Torres M., Desouza C., Gabrielli B.; RT "Cyclin A/cdk2 coordinates centrosomal and nuclear mitotic events."; RL Oncogene 27:4261-4268(2008). RN [32] RP INTERACTION WITH CACUL1. RX PubMed=19829063; DOI=10.4161/cc.8.21.9955; RA Kong Y., Nan K., Yin Y.; RT "Identification and characterization of CAC1 as a novel CDK2-associated RT cullin."; RL Cell Cycle 8:3552-3561(2009). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [36] RP FUNCTION IN VITAMIN D-MEDIATED GROWTH INHIBITION, SUBCELLULAR LOCATION, RP ACTIVITY REGULATION, AND PHOSPHORYLATION AT THR-160. RX PubMed=20147522; DOI=10.1210/en.2009-1116; RA Flores O., Wang Z., Knudsen K.E., Burnstein K.L.; RT "Nuclear targeting of cyclin-dependent kinase 2 reveals essential roles of RT cyclin-dependent kinase 2 localization and cyclin E in vitamin D-mediated RT growth inhibition."; RL Endocrinology 151:896-908(2010). RN [37] RP FUNCTION, AND S-NITROSYLATION. RX PubMed=20079829; DOI=10.1016/j.freeradbiomed.2010.01.004; RA Kumar S., Barthwal M.K., Dikshit M.; RT "Cdk2 nitrosylation and loss of mitochondrial potential mediate NO- RT dependent biphasic effect on HL-60 cell cycle."; RL Free Radic. Biol. Med. 48:851-861(2010). RN [38] RP PHOSPHORYLATION AT THR-160 BY CAK, AND DEPHOSPHORYLATION BY CDC25A. RX PubMed=20360007; DOI=10.1074/jbc.m109.096552; RA Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.; RT "Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at RT the G2/M transition."; RL J. Biol. Chem. 285:16978-16990(2010). RN [39] RP FUNCTION AS EZH2 KINASE. RX PubMed=20935635; DOI=10.1038/ncb2116; RA Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A., RA Simon J.A., Huang H.; RT "Cyclin-dependent kinases regulate epigenetic gene silencing through RT phosphorylation of EZH2."; RL Nat. Cell Biol. 12:1108-1114(2010). RN [40] RP FUNCTION IN DNA DAMAGE CHECKPOINT. RX PubMed=20195506; DOI=10.1371/journal.pgen.1000863; RA Chung J.H., Bunz F.; RT "Cdk2 is required for p53-independent G2/M checkpoint control."; RL PLoS Genet. 6:E1000863-E1000863(2010). RN [41] RP FUNCTION AS MYC KINASE. RX PubMed=19966300; DOI=10.1073/pnas.0900121106; RA Hydbring P., Bahram F., Su Y., Tronnersjoe S., Hoegstrand K., RA von der Lehr N., Sharifi H.R., Lilischkis R., Hein N., Wu S., Vervoorts J., RA Henriksson M., Grandien A., Luescher B., Larsson L.-G.; RT "Phosphorylation by Cdk2 is required for Myc to repress Ras-induced RT senescence in cotransformation."; RL Proc. Natl. Acad. Sci. U.S.A. 107:58-63(2010). RN [42] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [43] RP INTERACTION WITH CEP63. RX PubMed=21406398; DOI=10.1158/0008-5472.can-10-2684; RA Loffler H., Fechter A., Matuszewska M., Saffrich R., Mistrik M., RA Marhold J., Hornung C., Westermann F., Bartek J., Kramer A.; RT "Cep63 recruits Cdk1 to the centrosome: implications for regulation of RT mitotic entry, centrosome amplification, and genome maintenance."; RL Cancer Res. 71:2129-2139(2011). RN [44] RP FUNCTION AS CTNNB1 KINASE, SUBCELLULAR LOCATION, AND INTERACTION WITH PTPN6 RP AND CTNNB1. RX PubMed=21262353; DOI=10.1016/j.cellsig.2011.01.019; RA Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A., RA Olivier M., Beauchemin N., Faure R.L.; RT "Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and RT regulates insulin internalization."; RL Cell. Signal. 23:911-919(2011). RN [45] RP INHIBITORS. RX PubMed=21684737; DOI=10.1016/j.bmcl.2011.05.081; RA Lee J., Kim K.H., Jeong S.; RT "Discovery of a novel class of 2-aminopyrimidines as CDK1 and CDK2 RT inhibitors."; RL Bioorg. Med. Chem. Lett. 21:4203-4205(2011). RN [46] RP FUNCTION AS USP37 KINASE. RX PubMed=21596315; DOI=10.1016/j.molcel.2011.03.027; RA Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., RA Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.; RT "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and RT promote S phase entry."; RL Mol. Cell 42:511-523(2011). RN [47] RP FUNCTION IN CELL CYCLE REGULATION. RX PubMed=21319273; DOI=10.1002/stem.620; RA Neganova I., Vilella F., Atkinson S.P., Lloret M., Passos J.F., RA von Zglinicki T., O'Connor J.-E., Burks D., Jones R., Armstrong L., RA Lako M.; RT "An important role for CDK2 in G1 to S checkpoint activation and DNA damage RT response in human embryonic stem cells."; RL Stem Cells 29:651-659(2011). RN [48] RP REVIEW ON DNA REPAIR, AND INTERACTION WITH CDKN1A/P21. RX PubMed=19445729; DOI=10.1186/1747-1028-4-9; RA Satyanarayana A., Kaldis P.; RT "A dual role of Cdk2 in DNA damage response."; RL Cell Div. 4:9-9(2009). RN [49] RP REVIEW ON CELL CYCLE CONTROL, INHIBITORS, AND GENE FAMILY. RX PubMed=19238148; DOI=10.1038/nrc2602; RA Malumbres M., Barbacid M.; RT "Cell cycle, CDKs and cancer: a changing paradigm."; RL Nat. Rev. Cancer 9:153-166(2009). RN [50] RP REVIEW, AND GENE FAMILY. RX PubMed=19561645; DOI=10.1038/onc.2009.170; RA Satyanarayana A., Kaldis P.; RT "Mammalian cell-cycle regulation: several Cdks, numerous cyclins and RT diverse compensatory mechanisms."; RL Oncogene 28:2925-2939(2009). RN [51] RP REVIEW ON SENESCENCE. RX PubMed=20713526; DOI=10.1158/0008-5472.can-10-1383; RA Hydbring P., Larsson L.-G.; RT "Tipping the balance: Cdk2 enables Myc to suppress senescence."; RL Cancer Res. 70:6687-6691(2010). RN [52] RP REVIEW ON INHIBITORS. RX PubMed=21517772; DOI=10.2174/092986711795590110; RA Wang Q., Su L., Liu N., Zhang L., Xu W., Fang H.; RT "Cyclin dependent kinase 1 inhibitors: a review of recent progress."; RL Curr. Med. Chem. 18:2025-2043(2011). RN [53] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [54] RP INTERACTION WITH CYCLIN E; CYCLIN A AND CDK2AP2, AND PHOSPHORYLATION. RX PubMed=23781148; DOI=10.7150/ijbs.5763; RA Liu Q., Liu X., Gao J., Shi X., Hu X., Wang S., Luo Y.; RT "Overexpression of DOC-1R inhibits cell cycle G1/S transition by repressing RT CDK2 expression and activation."; RL Int. J. Biol. Sci. 9:541-549(2013). RN [55] RP FUNCTION. RX PubMed=29203878; DOI=10.1038/s41467-017-02114-x; RA Batenburg N.L., Walker J.R., Noordermeer S.M., Moatti N., Durocher D., RA Zhu X.D.; RT "ATM and CDK2 control chromatin remodeler CSB to inhibit RIF1 in DSB repair RT pathway choice."; RL Nat. Commun. 8:1921-1921(2017). RN [56] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=8510751; DOI=10.1038/363595a0; RA de Bondt H.L., Rosenblatt J., Jancarik J., Jones H.D., Morgan D.O., RA Kim S.-H.; RT "Crystal structure of cyclin-dependent kinase 2."; RL Nature 363:595-602(1993). RN [57] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CYCLIN A. RX PubMed=7630397; DOI=10.1038/376313a0; RA Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., RA Pavletich N.P.; RT "Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 RT complex."; RL Nature 376:313-320(1995). RN [58] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITG CKS1. RX PubMed=8601310; DOI=10.1016/s0092-8674(00)81065-x; RA Bourne Y., Watson M.H., Hickey M.J., Holmes W., Rocque W., Reed S.I., RA Tainer J.A.; RT "Crystal structure and mutational analysis of the human CDK2 kinase complex RT with cell cycle-regulatory protein CksHs1."; RL Cell 84:863-874(1996). RN [59] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=8917641; DOI=10.1021/jm960402a; RA Schulze-Gahmen U., de Bondt H.L., Kim S.-H.; RT "High-resolution crystal structures of human cyclin-dependent kinase 2 with RT and without ATP: bound waters and natural ligand as guides for inhibitor RT design."; RL J. Med. Chem. 39:4540-4546(1996). RN [60] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CCNA2 AND CDKN1B. RX PubMed=8684460; DOI=10.1038/382325a0; RA Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.; RT "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound RT to the cyclin A-Cdk2 complex."; RL Nature 382:325-331(1996). RN [61] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CG2A. RX PubMed=8756328; DOI=10.1038/nsb0896-696; RA Russo A.A., Jeffrey P.D., Pavletich N.P.; RT "Structural basis of cyclin-dependent kinase activation by RT phosphorylation."; RL Nat. Struct. Biol. 3:696-700(1996). RN [62] RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH L868276. RX PubMed=8610110; DOI=10.1073/pnas.93.7.2735; RA de Azevedo W.F. Jr., Mueller-Dieckmann H.-J., Schulze-Gahmen U., RA Worland P.J., Sausville E., Kim S.-H.; RT "Structural basis for specificity and potency of a flavonoid inhibitor of RT human CDK2, a cell cycle kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 93:2735-2740(1996). RN [63] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH STAUROSPORINE, AND RP ACTIVITY REGULATION. RX PubMed=9334743; DOI=10.1038/nsb1097-796; RA Lawrie A.M., Noble M.E.M., Tunnah P., Brown N.R., Johnson L.N., RA Endicott J.A.; RT "Protein kinase inhibition by staurosporine revealed in details of the RT molecular interaction with CDK2."; RL Nat. Struct. Biol. 4:796-801(1997). RN [64] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). RX PubMed=9677190; DOI=10.1126/science.281.5376.533; RA Gray N.S., Wodicka L., Thunnissen A.-M.W.H., Norman T.C., Kwon S., RA Espinoza F.H., Morgan D.O., Barnes G., Leclerc S., Meijer L., Kim S.H., RA Lockhart D.J., Schultz P.G.; RT "Exploiting chemical libraries, structure, and genomics in the search for RT kinase inhibitors."; RL Science 281:533-538(1998). RN [65] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND RP PHOSPHORYLATION AT THR-160. RX PubMed=16325401; DOI=10.1016/j.bmcl.2005.11.048; RA Richardson C.M., Williamson D.S., Parratt M.J., Borgognoni J., RA Cansfield A.D., Dokurno P., Francis G.L., Howes R., Moore J.D., RA Murray J.B., Robertson A., Surgenor A.E., Torrance C.J.; RT "Triazolo[1,5-a]pyrimidines as novel CDK2 inhibitors: protein structure- RT guided design and SAR."; RL Bioorg. Med. Chem. Lett. 16:1353-1357(2006). RN [66] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND RP PHOSPHORYLATION AT THR-160. RX PubMed=17570665; DOI=10.1016/j.bmcl.2007.04.110; RA Richardson C.M., Nunns C.L., Williamson D.S., Parratt M.J., Dokurno P., RA Howes R., Borgognoni J., Drysdale M.J., Finch H., Hubbard R.E., RA Jackson P.S., Kierstan P., Lentzen G., Moore J.D., Murray J.B., RA Simmonite H., Surgenor A.E., Torrance C.J.; RT "Discovery of a potent CDK2 inhibitor with a novel binding mode, using RT virtual screening and initial, structure-guided lead scoping."; RL Bioorg. Med. Chem. Lett. 17:3880-3885(2007). RN [67] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-288 IN COMPLEX WITH CCNB1, AND RP FUNCTION. RX PubMed=17495531; DOI=10.4161/cc.6.11.4278; RA Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.; RT "Cyclin B and cyclin A confer different substrate recognition properties on RT CDK2."; RL Cell Cycle 6:1350-1359(2007). RN [68] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ATP, AND RP PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160. RX PubMed=17095507; DOI=10.1074/jbc.m609151200; RA Welburn J.P.I., Tucker J.A., Johnson T., Lindert L., Morgan M., Willis A., RA Noble M.E.M., Endicott J.A.; RT "How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent RT kinase 2-cyclin A."; RL J. Biol. Chem. 282:3173-3181(2007). RN [69] RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) IN COMPLEX WITH INHIBITORS. RX PubMed=17937404; DOI=10.1002/bip.20868; RA Fischmann T.O., Hruza A., Duca J.S., Ramanathan L., Mayhood T., RA Windsor W.T., Le H.V., Guzi T.J., Dwyer M.P., Paruch K., Doll R.J., RA Lees E., Parry D., Seghezzi W., Madison V.; RT "Structure-guided discovery of cyclin-dependent kinase inhibitors."; RL Biopolymers 89:372-379(2008). RN [70] RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH INHIBITORS. RX PubMed=18656911; DOI=10.1021/jm800382h; RA Wyatt P.G., Woodhead A.J., Berdini V., Boulstridge J.A., Carr M.G., RA Cross D.M., Davis D.J., Devine L.A., Early T.R., Feltell R.E., Lewis E.J., RA McMenamin R.L., Navarro E.F., O'Brien M.A., O'Reilly M., Reule M., RA Saxty G., Seavers L.C., Smith D.M., Squires M.S., Trewartha G., RA Walker M.T., Woolford A.J.; RT "Identification of N-(4-piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H- RT pyrazole-3-carboxamide (AT7519), a novel cyclin dependent kinase inhibitor RT using fragment-based X-ray crystallography and structure based drug RT design."; RL J. Med. Chem. 51:4986-4999(2008). RN [71] RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-296 IN COMPLEX WITH ATP AND RP MAGNESIUM, COFACTOR, AND PHOSPHORYLATION AT THR-160. RX PubMed=21565702; DOI=10.1016/j.str.2011.02.016; RA Bao Z.Q., Jacobsen D.M., Young M.A.; RT "Briefly bound to activate: transient binding of a second catalytic RT magnesium activates the structure and dynamics of CDK2 kinase for RT catalysis."; RL Structure 19:675-690(2011). RN [72] {ECO:0007744|PDB:5UQ1, ECO:0007744|PDB:5UQ2, ECO:0007744|PDB:5UQ3} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEXES WITH SPDYA AND CDKN1B, RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH SPDYA RP AND CDKN1B, AND PHOSPHORYLATION AT THR-160. RX PubMed=28666995; DOI=10.15252/embj.201796905; RA McGrath D.A., Fifield B.A., Marceau A.H., Tripathi S., Porter L.A., RA Rubin S.M.; RT "Structural basis of divergent cyclin-dependent kinase activation by RT Spy1/RINGO proteins."; RL EMBO J. 36:2251-2262(2017). RN [73] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-45 AND SER-290. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [74] RP INTERACTION WITH ANKRD17. RX PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037; RA Menning M., Kufer T.A.; RT "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and RT Nod2-mediated inflammatory responses."; RL FEBS Lett. 587:2137-2142(2013). CC -!- FUNCTION: Serine/threonine-protein kinase involved in the control of CC the cell cycle; essential for meiosis, but dispensable for mitosis. CC Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, CC NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the CC G1-S transition to promote the E2F transcriptional program and the CC initiation of DNA synthesis, and modulates G2 progression; controls the CC timing of entry into mitosis/meiosis by controlling the subsequent CC activation of cyclin B/CDK1 by phosphorylation, and coordinates the CC activation of cyclin B/CDK1 at the centrosome and in the nucleus. CC Crucial role in orchestrating a fine balance between cellular CC proliferation, cell death, and DNA repair in human embryonic stem cells CC (hESCs). Activity of CDK2 is maximal during S phase and G2; activated CC by interaction with cyclin E during the early stages of DNA synthesis CC to permit G1-S transition, and subsequently activated by cyclin A2 CC (cyclin A1 in germ cells) during the late stages of DNA replication to CC drive the transition from S phase to mitosis, the G2 phase. EZH2 CC phosphorylation promotes H3K27me3 maintenance and epigenetic gene CC silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 CC prevents oxidative stress-mediated Ras-induced senescence by CC phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that CC prevents cells with damaged DNA from initiating mitosis; regulates CC homologous recombination-dependent repair by phosphorylating BRCA2, CC this phosphorylation is low in S phase when recombination is active, CC but increases as cells progress towards mitosis. In response to DNA CC damage, double-strand break repair by homologous recombination a CC reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of CC RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin CC E/CDK2 promotes its dissociates from unduplicated centrosomes, thus CC initiating centrosome duplication. Cyclin E/CDK2-mediated CC phosphorylation of NPAT at G1-S transition and until prophase CC stimulates the NPAT-mediated activation of histone gene transcription CC during S phase. Required for vitamin D-mediated growth inhibition by CC being itself inactivated. Involved in the nitric oxide- (NO) mediated CC signaling in a nitrosylation/activation-dependent manner. USP37 is CC activated by phosphorylation and thus triggers G1-S transition. CTNNB1 CC phosphorylation regulates insulin internalization. Phosphorylates FOXP3 CC and negatively regulates its transcriptional activity and protein CC stability (By similarity). Phosphorylates CDK2AP2 (PubMed:12944431). CC Phosphorylates ERCC6 which is essential for its chromatin remodeling CC activity at DNA double-strand breaks (PubMed:29203878). CC {ECO:0000250|UniProtKB:P97377, ECO:0000269|PubMed:10499802, CC ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:10995386, CC ECO:0000269|PubMed:10995387, ECO:0000269|PubMed:11051553, CC ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:12944431, CC ECO:0000269|PubMed:15800615, ECO:0000269|PubMed:17495531, CC ECO:0000269|PubMed:18372919, ECO:0000269|PubMed:19966300, CC ECO:0000269|PubMed:20079829, ECO:0000269|PubMed:20147522, CC ECO:0000269|PubMed:20195506, ECO:0000269|PubMed:20935635, CC ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:21319273, CC ECO:0000269|PubMed:21596315, ECO:0000269|PubMed:28666995, CC ECO:0000269|PubMed:29203878}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CC Evidence={ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:28666995, CC ECO:0000269|PubMed:9030781}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.22; Evidence={ECO:0000269|PubMed:1396589, CC ECO:0000269|PubMed:28666995, ECO:0000269|PubMed:9030781}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:21565702}; CC Note=Binds 2 Mg(2+) ions. {ECO:0000269|PubMed:21565702}; CC -!- ACTIVITY REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates CC the enzyme, while phosphorylation at Thr-160 activates it CC (PubMed:1396589). Inhibited by 1,25-dihydroxyvitamin D(3) (1,25- CC (OH)(2)D(3)), AG-024322, N-(4-Piperidinyl)-4-(2,6- CC dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), R547 (Ro- CC 4584820), purine, pyrimidine and pyridine derivatives, 2- CC aminopyrimidines, paullones, thiazo derivatives, macrocyclic CC quinoxalin-2-one, pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5- CC a]pyrimidine, 2-(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9- CC isopropylpurine (roscovitine, seliciclib and CYC202), SNS-032 (BMS- CC 387032), triazolo[1,5-a]pyrimidines, staurosporine and olomoucine. CC Stimulated by MYC. Inactivated by CDKN1A (p21). CC {ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:20147522, CC ECO:0000269|PubMed:28666995, ECO:0000269|PubMed:9030781, CC ECO:0000269|PubMed:9334743}. CC -!- SUBUNIT: Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts CC with CABLES1 (By similarity). Interacts with UHRF2. Part of a complex CC consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo CC proteins SPDYA and SPDYC (PubMed:15611625). Interaction with SPDYA CC promotes kinase activation via a conformation change that alleviates CC obstruction of the substrate-binding cleft by the T-loop CC (PubMed:28666995). Found in a complex with both SPDYA and CDKN1B/KIP1 CC (PubMed:12972555, PubMed:28666995). Binds to RB1 and CDK7. Binding to CC CDKN1A (p21) leads to CDK2/cyclin E inactivation at the G1-S phase DNA CC damage checkpoint, thereby arresting cells at the G1-S transition CC during DNA repair. Associated with PTPN6 and beta-catenin/CTNNB1. CC Interacts with CACUL1. May interact with CEP63. Interacts with ANKRD17. CC Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Forms a CC ternary complex with CCNA2 and CDKN1B; CDKN1B inhibits the kinase CC activity of CDK2 through conformational rearrangements CC (PubMed:8684460). Interacts with cyclins A, B1, B3, D, or E CC (PubMed:10499802, PubMed:10884347, PubMed:12185076, PubMed:23781148). CC Interacts with CDK2AP2 (PubMed:23781148). CC {ECO:0000250|UniProtKB:P97377, ECO:0000250|UniProtKB:Q63699, CC ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:10884347, CC ECO:0000269|PubMed:11980914, ECO:0000269|PubMed:12185076, CC ECO:0000269|PubMed:12839962, ECO:0000269|PubMed:12972555, CC ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:15178429, CC ECO:0000269|PubMed:15611625, ECO:0000269|PubMed:16325401, CC ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17373709, CC ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:17570665, CC ECO:0000269|PubMed:17937404, ECO:0000269|PubMed:18656911, CC ECO:0000269|PubMed:19445729, ECO:0000269|PubMed:19829063, CC ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:21406398, CC ECO:0000269|PubMed:21565702, ECO:0000269|PubMed:23711367, CC ECO:0000269|PubMed:23781148, ECO:0000269|PubMed:28666995, CC ECO:0000269|PubMed:7630397, ECO:0000269|PubMed:8610110, CC ECO:0000269|PubMed:8684460, ECO:0000269|PubMed:8756328, CC ECO:0000269|PubMed:9334743}. CC -!- INTERACTION: CC P24941; P20248: CCNA2; NbExp=28; IntAct=EBI-375096, EBI-457097; CC P24941; O95067: CCNB2; NbExp=4; IntAct=EBI-375096, EBI-375024; CC P24941; P24385: CCND1; NbExp=6; IntAct=EBI-375096, EBI-375001; CC P24941; P24864: CCNE1; NbExp=20; IntAct=EBI-375096, EBI-519526; CC P24941; O96020: CCNE2; NbExp=11; IntAct=EBI-375096, EBI-375033; CC P24941; P51946: CCNH; NbExp=4; IntAct=EBI-375096, EBI-741406; CC P24941; P50613: CDK7; NbExp=3; IntAct=EBI-375096, EBI-1245958; CC P24941; P38936: CDKN1A; NbExp=28; IntAct=EBI-375096, EBI-375077; CC P24941; P46527: CDKN1B; NbExp=27; IntAct=EBI-375096, EBI-519280; CC P24941; Q16667: CDKN3; NbExp=7; IntAct=EBI-375096, EBI-1031527; CC P24941; P61024: CKS1B; NbExp=20; IntAct=EBI-375096, EBI-456371; CC P24941; Q09472: EP300; NbExp=6; IntAct=EBI-375096, EBI-447295; CC P24941; Q969H0-4: FBXW7; NbExp=2; IntAct=EBI-375096, EBI-6502391; CC P24941; P22607: FGFR3; NbExp=3; IntAct=EBI-375096, EBI-348399; CC P24941; Q14957: GRIN2C; NbExp=3; IntAct=EBI-375096, EBI-8285963; CC P24941; P06396: GSN; NbExp=3; IntAct=EBI-375096, EBI-351506; CC P24941; P01112: HRAS; NbExp=3; IntAct=EBI-375096, EBI-350145; CC P24941; Q9Y6K9: IKBKG; NbExp=4; IntAct=EBI-375096, EBI-81279; CC P24941; O95835: LATS1; NbExp=4; IntAct=EBI-375096, EBI-444209; CC P24941; Q8TD08: MAPK15; NbExp=4; IntAct=EBI-375096, EBI-1383794; CC P24941; P06400: RB1; NbExp=3; IntAct=EBI-375096, EBI-491274; CC P24941; Q9BY12: SCAPER; NbExp=3; IntAct=EBI-375096, EBI-308519; CC P24941; Q9UQR0: SCML2; NbExp=3; IntAct=EBI-375096, EBI-2513111; CC P24941; Q9UQR0-1: SCML2; NbExp=7; IntAct=EBI-375096, EBI-16087037; CC P24941; Q9UBI4: STOML1; NbExp=2; IntAct=EBI-375096, EBI-2681162; CC P24941; Q96PU4: UHRF2; NbExp=5; IntAct=EBI-375096, EBI-625304; CC P24941; P30274: CCNA2; Xeno; NbExp=2; IntAct=EBI-375096, EBI-15688654; CC P24941; P51943: Ccna2; Xeno; NbExp=2; IntAct=EBI-375096, EBI-846980; CC P24941; P03129: E7; Xeno; NbExp=2; IntAct=EBI-375096, EBI-866453; CC P24941; Q08619: Ifi205b; Xeno; NbExp=2; IntAct=EBI-375096, EBI-8064290; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome. Nucleus, Cajal body. Cytoplasm. Endosome. CC Note=Localized at the centrosomes in late G2 phase after separation of CC the centrosomes but before the start of prophase. Nuclear-cytoplasmic CC trafficking is mediated during the inhibition by 1,25-(OH)(2)D(3). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P24941-1; Sequence=Displayed; CC Name=2; Synonyms=CDK2deltaT; CC IsoId=P24941-2; Sequence=VSP_041998; CC -!- INDUCTION: Induced transiently by TGFB1 at an early phase of TGFB1- CC mediated apoptosis. CC -!- PTM: Phosphorylated at Thr-160 by CDK7 in a CAK complex CC (PubMed:28666995). Phosphorylation at Thr-160 promotes kinase activity, CC whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase CC activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases CC before being dephosphorylated by CDC25A. {ECO:0000269|PubMed:11113184, CC ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, CC ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, CC ECO:0000269|PubMed:17373709, ECO:0000269|PubMed:17570665, CC ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, CC ECO:0000269|PubMed:21565702, ECO:0000269|PubMed:23781148, CC ECO:0000305|PubMed:28666995}. CC -!- PTM: Nitrosylated after treatment with nitric oxide (DETA-NO). CC {ECO:0000269|PubMed:20079829}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/cdk2/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X61622; CAA43807.1; -; mRNA. DR EMBL; X62071; CAA43985.1; -; mRNA. DR EMBL; M68520; AAA35667.1; -; mRNA. DR EMBL; AB012305; BAA32794.1; -; mRNA. DR EMBL; BT006821; AAP35467.1; -; mRNA. DR EMBL; AF512553; AAM34794.1; -; Genomic_DNA. DR EMBL; AK291941; BAF84630.1; -; mRNA. DR EMBL; AC025162; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC034102; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW96858.1; -; Genomic_DNA. DR EMBL; BC003065; AAH03065.1; -; mRNA. DR CCDS; CCDS8898.1; -. [P24941-1] DR CCDS; CCDS8899.1; -. [P24941-2] DR PIR; A41227; A41227. DR RefSeq; NP_001277159.1; NM_001290230.1. DR RefSeq; NP_001789.2; NM_001798.4. [P24941-1] DR RefSeq; NP_439892.2; NM_052827.3. [P24941-2] DR PDB; 1AQ1; X-ray; 2.00 A; A=1-298. DR PDB; 1B38; X-ray; 2.00 A; A=1-298. DR PDB; 1B39; X-ray; 2.10 A; A=1-298. DR PDB; 1BUH; X-ray; 2.60 A; A=1-298. DR PDB; 1CKP; X-ray; 2.05 A; A=1-298. DR PDB; 1DI8; X-ray; 2.20 A; A=1-298. DR PDB; 1DM2; X-ray; 2.10 A; A=1-298. DR PDB; 1E1V; X-ray; 1.95 A; A=1-298. DR PDB; 1E1X; X-ray; 1.85 A; A=1-298. DR PDB; 1E9H; X-ray; 2.50 A; A/C=1-296. DR PDB; 1F5Q; X-ray; 2.50 A; A/C=1-298. DR PDB; 1FIN; X-ray; 2.30 A; A/C=1-298. DR PDB; 1FQ1; X-ray; 3.00 A; B=1-298. DR PDB; 1FVT; X-ray; 2.20 A; A=1-298. DR PDB; 1FVV; X-ray; 2.80 A; A/C=1-298. DR PDB; 1G5S; X-ray; 2.61 A; A=1-298. DR PDB; 1GIH; X-ray; 2.80 A; A=1-298. DR PDB; 1GII; X-ray; 2.00 A; A=1-298. DR PDB; 1GIJ; X-ray; 2.20 A; A=1-298. DR PDB; 1GY3; X-ray; 2.70 A; A/C=1-296. DR PDB; 1GZ8; X-ray; 1.30 A; A=1-298. DR PDB; 1H00; X-ray; 1.60 A; A=1-298. DR PDB; 1H01; X-ray; 1.79 A; A=1-298. DR PDB; 1H07; X-ray; 1.85 A; A=1-298. DR PDB; 1H08; X-ray; 1.80 A; A=1-298. DR PDB; 1H0V; X-ray; 1.90 A; A=1-298. DR PDB; 1H0W; X-ray; 2.10 A; A=1-298. DR PDB; 1H1P; X-ray; 2.10 A; A/C=1-298. DR PDB; 1H1Q; X-ray; 2.50 A; A/C=1-298. DR PDB; 1H1R; X-ray; 2.00 A; A/C=1-298. DR PDB; 1H1S; X-ray; 2.00 A; A/C=1-298. DR PDB; 1H24; X-ray; 2.50 A; A/C=1-298. DR PDB; 1H25; X-ray; 2.50 A; A/C=1-298. DR PDB; 1H26; X-ray; 2.24 A; A/C=1-298. DR PDB; 1H27; X-ray; 2.20 A; A/C=1-298. DR PDB; 1H28; X-ray; 2.80 A; A/C=1-298. DR PDB; 1HCK; X-ray; 1.90 A; A=1-298. DR PDB; 1HCL; X-ray; 1.80 A; A=1-298. DR PDB; 1JST; X-ray; 2.60 A; A/C=1-298. DR PDB; 1JSU; X-ray; 2.30 A; A=1-298. DR PDB; 1JSV; X-ray; 1.96 A; A=1-298. DR PDB; 1JVP; X-ray; 1.53 A; P=1-298. DR PDB; 1KE5; X-ray; 2.20 A; A=1-298. DR PDB; 1KE6; X-ray; 2.00 A; A=1-298. DR PDB; 1KE7; X-ray; 2.00 A; A=1-298. DR PDB; 1KE8; X-ray; 2.00 A; A=1-298. DR PDB; 1KE9; X-ray; 2.00 A; A=1-298. DR PDB; 1OGU; X-ray; 2.60 A; A/C=1-298. DR PDB; 1OI9; X-ray; 2.10 A; A/C=1-298. DR PDB; 1OIQ; X-ray; 2.31 A; A=1-298. DR PDB; 1OIR; X-ray; 1.91 A; A=1-298. DR PDB; 1OIT; X-ray; 1.60 A; A=1-298. DR PDB; 1OIU; X-ray; 2.00 A; A/C=1-298. DR PDB; 1OIY; X-ray; 2.40 A; A/C=1-298. DR PDB; 1OKV; X-ray; 2.40 A; A/C=1-298. DR PDB; 1OKW; X-ray; 2.50 A; A/C=1-298. DR PDB; 1OL1; X-ray; 2.90 A; A/C=1-298. DR PDB; 1OL2; X-ray; 2.60 A; A/C=1-298. DR PDB; 1P2A; X-ray; 2.50 A; A=1-298. DR PDB; 1P5E; X-ray; 2.22 A; A/C=1-298. DR PDB; 1PF8; X-ray; 2.51 A; A=1-298. DR PDB; 1PKD; X-ray; 2.30 A; A/C=1-296. DR PDB; 1PW2; X-ray; 1.95 A; A=1-298. DR PDB; 1PXI; X-ray; 1.95 A; A=1-298. DR PDB; 1PXJ; X-ray; 2.30 A; A=1-298. DR PDB; 1PXK; X-ray; 2.80 A; A=1-298. DR PDB; 1PXL; X-ray; 2.50 A; A=1-298. DR PDB; 1PXM; X-ray; 2.53 A; A=1-298. DR PDB; 1PXN; X-ray; 2.50 A; A=1-298. DR PDB; 1PXO; X-ray; 1.96 A; A=1-298. DR PDB; 1PXP; X-ray; 2.30 A; A=1-298. DR PDB; 1PYE; X-ray; 2.00 A; A=1-298. DR PDB; 1QMZ; X-ray; 2.20 A; A/C=1-298. DR PDB; 1R78; X-ray; 2.00 A; A=1-298. DR PDB; 1URC; X-ray; 2.60 A; A/C=1-298. DR PDB; 1URW; X-ray; 1.60 A; A=1-298. DR PDB; 1V1K; X-ray; 2.31 A; A=1-298. DR PDB; 1VYW; X-ray; 2.30 A; A/C=1-298. DR PDB; 1VYZ; X-ray; 2.21 A; A=1-298. DR PDB; 1W0X; X-ray; 2.20 A; C=1-298. DR PDB; 1W8C; X-ray; 2.05 A; A=1-298. DR PDB; 1W98; X-ray; 2.15 A; A=1-297. DR PDB; 1WCC; X-ray; 2.20 A; A=1-298. DR PDB; 1Y8Y; X-ray; 2.00 A; A=1-298. DR PDB; 1Y91; X-ray; 2.15 A; A=1-298. DR PDB; 1YKR; X-ray; 1.80 A; A=1-298. DR PDB; 2A0C; X-ray; 1.95 A; X=1-298. DR PDB; 2A4L; X-ray; 2.40 A; A=1-298. DR PDB; 2B52; X-ray; 1.88 A; A=1-298. DR PDB; 2B53; X-ray; 2.00 A; A=1-298. DR PDB; 2B54; X-ray; 1.85 A; A=1-298. DR PDB; 2B55; X-ray; 1.85 A; A=1-298. DR PDB; 2BHE; X-ray; 1.90 A; A=1-298. DR PDB; 2BHH; X-ray; 2.60 A; A=1-298. DR PDB; 2BKZ; X-ray; 2.60 A; A/C=1-298. DR PDB; 2BPM; X-ray; 2.40 A; A/C=1-298. DR PDB; 2BTR; X-ray; 1.85 A; A=1-298. DR PDB; 2BTS; X-ray; 1.99 A; A=1-298. DR PDB; 2C4G; X-ray; 2.70 A; A/C=1-298. DR PDB; 2C5N; X-ray; 2.10 A; A/C=1-298. DR PDB; 2C5O; X-ray; 2.10 A; A/C=1-298. DR PDB; 2C5V; X-ray; 2.90 A; A/C=1-298. DR PDB; 2C5X; X-ray; 2.90 A; A/C=1-298. DR PDB; 2C5Y; X-ray; 2.25 A; A=1-298. DR PDB; 2C68; X-ray; 1.95 A; A=1-298. DR PDB; 2C69; X-ray; 2.10 A; A=1-298. DR PDB; 2C6I; X-ray; 1.80 A; A=1-298. DR PDB; 2C6K; X-ray; 1.90 A; A=1-298. DR PDB; 2C6L; X-ray; 2.30 A; A=1-298. DR PDB; 2C6M; X-ray; 1.90 A; A=1-298. DR PDB; 2C6O; X-ray; 2.10 A; A=1-298. DR PDB; 2C6T; X-ray; 2.61 A; A/C=1-298. DR PDB; 2CCH; X-ray; 1.70 A; A/C=1-298. DR PDB; 2CCI; X-ray; 2.70 A; A/C=1-298. DR PDB; 2CJM; X-ray; 2.30 A; A/C=1-298. DR PDB; 2CLX; X-ray; 1.80 A; A=1-298. DR PDB; 2DS1; X-ray; 2.00 A; A=1-298. DR PDB; 2DUV; X-ray; 2.20 A; A=1-298. DR PDB; 2EXM; X-ray; 1.80 A; A=1-298. DR PDB; 2FVD; X-ray; 1.85 A; A=1-298. DR PDB; 2G9X; X-ray; 2.50 A; A/C=1-298. DR PDB; 2I40; X-ray; 2.80 A; A/C=1-298. DR PDB; 2IW6; X-ray; 2.30 A; A/C=1-298. DR PDB; 2IW8; X-ray; 2.30 A; A/C=1-298. DR PDB; 2IW9; X-ray; 2.00 A; A/C=1-298. DR PDB; 2J9M; X-ray; 2.50 A; A=1-298. DR PDB; 2JGZ; X-ray; 2.90 A; A=1-288. DR PDB; 2R3F; X-ray; 1.50 A; A=1-298. DR PDB; 2R3G; X-ray; 1.55 A; A=1-298. DR PDB; 2R3H; X-ray; 1.50 A; A=1-298. DR PDB; 2R3I; X-ray; 1.28 A; A=1-298. DR PDB; 2R3J; X-ray; 1.65 A; A=1-298. DR PDB; 2R3K; X-ray; 1.70 A; A=1-298. DR PDB; 2R3L; X-ray; 1.65 A; A=1-298. DR PDB; 2R3M; X-ray; 1.70 A; A=1-298. DR PDB; 2R3N; X-ray; 1.63 A; A=1-298. DR PDB; 2R3O; X-ray; 1.80 A; A=1-298. DR PDB; 2R3P; X-ray; 1.66 A; A=1-298. DR PDB; 2R3Q; X-ray; 1.35 A; A=1-298. DR PDB; 2R3R; X-ray; 1.47 A; A=1-298. DR PDB; 2R64; X-ray; 2.30 A; A=1-298. DR PDB; 2UUE; X-ray; 2.06 A; A/C=1-298. DR PDB; 2UZB; X-ray; 2.70 A; A/C=1-298. DR PDB; 2UZD; X-ray; 2.72 A; A/C=1-298. DR PDB; 2UZE; X-ray; 2.40 A; A/C=1-298. DR PDB; 2UZL; X-ray; 2.40 A; A/C=1-298. DR PDB; 2UZN; X-ray; 2.30 A; A=1-298. DR PDB; 2UZO; X-ray; 2.30 A; A=1-298. DR PDB; 2V0D; X-ray; 2.20 A; A=1-298. DR PDB; 2V22; X-ray; 2.60 A; A/C=1-298. DR PDB; 2VTA; X-ray; 2.00 A; A=1-298. DR PDB; 2VTH; X-ray; 1.90 A; A=1-298. DR PDB; 2VTI; X-ray; 2.00 A; A=1-298. DR PDB; 2VTJ; X-ray; 2.20 A; A=1-298. DR PDB; 2VTL; X-ray; 2.00 A; A=1-298. DR PDB; 2VTM; X-ray; 2.25 A; A=1-298. DR PDB; 2VTN; X-ray; 2.20 A; A=1-298. DR PDB; 2VTO; X-ray; 2.19 A; A=1-298. DR PDB; 2VTP; X-ray; 2.15 A; A=1-298. DR PDB; 2VTQ; X-ray; 1.90 A; A=1-298. DR PDB; 2VTR; X-ray; 1.90 A; A=1-298. DR PDB; 2VTS; X-ray; 1.90 A; A=1-298. DR PDB; 2VTT; X-ray; 1.68 A; A=1-298. DR PDB; 2VU3; X-ray; 1.85 A; A=1-298. DR PDB; 2VV9; X-ray; 1.90 A; A=1-298. DR PDB; 2W05; X-ray; 1.90 A; A=1-298. DR PDB; 2W06; X-ray; 2.04 A; A=1-298. DR PDB; 2W17; X-ray; 2.15 A; A=1-298. DR PDB; 2W1H; X-ray; 2.15 A; A=1-298. DR PDB; 2WEV; X-ray; 2.30 A; A/C=1-298. DR PDB; 2WFY; X-ray; 2.53 A; A/C=1-298. DR PDB; 2WHB; X-ray; 2.90 A; A/C=1-298. DR PDB; 2WIH; X-ray; 2.50 A; A/C=1-298. DR PDB; 2WIP; X-ray; 2.80 A; A/C=1-298. DR PDB; 2WMA; X-ray; 2.80 A; A/C=1-298. DR PDB; 2WMB; X-ray; 2.60 A; A/C=1-298. DR PDB; 2WPA; X-ray; 2.51 A; A/C=1-298. DR PDB; 2WXV; X-ray; 2.60 A; A/C=1-298. DR PDB; 2X1N; X-ray; 2.75 A; A/C=1-298. DR PDB; 2XMY; X-ray; 1.90 A; A=1-298. DR PDB; 2XNB; X-ray; 1.85 A; A=1-298. DR PDB; 3BHT; X-ray; 2.00 A; A/C=1-298. DR PDB; 3BHU; X-ray; 2.30 A; A/C=1-298. DR PDB; 3BHV; X-ray; 2.10 A; A/C=1-298. DR PDB; 3DDP; X-ray; 2.70 A; A/C=1-298. DR PDB; 3DDQ; X-ray; 1.80 A; A/C=1-298. DR PDB; 3DOG; X-ray; 2.70 A; A/C=1-298. DR PDB; 3EID; X-ray; 3.15 A; A/C=1-298. DR PDB; 3EJ1; X-ray; 3.22 A; A/C=1-298. DR PDB; 3EOC; X-ray; 3.20 A; A/C=1-298. DR PDB; 3EZR; X-ray; 1.90 A; A=1-298. DR PDB; 3EZV; X-ray; 1.99 A; A=1-298. DR PDB; 3F5X; X-ray; 2.40 A; A/C=1-298. DR PDB; 3FZ1; X-ray; 1.90 A; A=1-298. DR PDB; 3IG7; X-ray; 1.80 A; A=1-298. DR PDB; 3IGG; X-ray; 1.80 A; A=1-298. DR PDB; 3LE6; X-ray; 2.00 A; A=1-298. DR PDB; 3LFN; X-ray; 2.28 A; A=1-298. DR PDB; 3LFQ; X-ray; 2.03 A; A=1-298. DR PDB; 3LFS; X-ray; 2.40 A; A=1-298. DR PDB; 3MY5; X-ray; 2.10 A; A/C=1-298. DR PDB; 3NS9; X-ray; 1.78 A; A=1-298. DR PDB; 3PJ8; X-ray; 1.96 A; A=1-298. DR PDB; 3PXF; X-ray; 1.80 A; A=1-298. DR PDB; 3PXQ; X-ray; 1.90 A; A=1-298. DR PDB; 3PXR; X-ray; 2.00 A; A=1-298. DR PDB; 3PXY; X-ray; 1.80 A; A=1-298. DR PDB; 3PXZ; X-ray; 1.70 A; A=1-298. DR PDB; 3PY0; X-ray; 1.75 A; A=1-298. DR PDB; 3PY1; X-ray; 2.05 A; A=1-298. DR PDB; 3QHR; X-ray; 2.17 A; A/C=1-296. DR PDB; 3QHW; X-ray; 1.91 A; A/C=1-296. DR PDB; 3QL8; X-ray; 1.90 A; A=1-298. DR PDB; 3QQF; X-ray; 1.75 A; A=1-298. DR PDB; 3QQG; X-ray; 1.90 A; A=1-298. DR PDB; 3QQH; X-ray; 1.87 A; A=1-298. DR PDB; 3QQJ; X-ray; 1.70 A; A=1-298. DR PDB; 3QQK; X-ray; 1.86 A; A=1-298. DR PDB; 3QQL; X-ray; 1.85 A; A=1-298. DR PDB; 3QRT; X-ray; 1.75 A; A=1-298. DR PDB; 3QRU; X-ray; 1.95 A; A=1-298. DR PDB; 3QTQ; X-ray; 1.80 A; A=1-298. DR PDB; 3QTR; X-ray; 1.85 A; A=1-298. DR PDB; 3QTS; X-ray; 1.90 A; A=1-298. DR PDB; 3QTU; X-ray; 1.82 A; A=1-298. DR PDB; 3QTW; X-ray; 1.85 A; A=1-298. DR PDB; 3QTX; X-ray; 1.95 A; A=1-298. DR PDB; 3QTZ; X-ray; 2.00 A; A=1-298. DR PDB; 3QU0; X-ray; 1.95 A; A=1-298. DR PDB; 3QWJ; X-ray; 1.75 A; A=1-298. DR PDB; 3QWK; X-ray; 1.85 A; A=1-298. DR PDB; 3QX2; X-ray; 1.75 A; A=1-298. DR PDB; 3QX4; X-ray; 1.92 A; A=1-298. DR PDB; 3QXO; X-ray; 1.75 A; A=1-298. DR PDB; 3QXP; X-ray; 1.75 A; A=1-298. DR PDB; 3QZF; X-ray; 2.00 A; A=1-298. DR PDB; 3QZG; X-ray; 1.75 A; A=1-298. DR PDB; 3QZH; X-ray; 1.95 A; A=1-298. DR PDB; 3QZI; X-ray; 1.75 A; A=1-298. DR PDB; 3R1Q; X-ray; 1.85 A; A=1-298. DR PDB; 3R1S; X-ray; 1.80 A; A=1-298. DR PDB; 3R1Y; X-ray; 1.80 A; A=1-298. DR PDB; 3R28; X-ray; 1.75 A; A=1-298. DR PDB; 3R6X; X-ray; 1.75 A; A=1-298. DR PDB; 3R71; X-ray; 1.75 A; A=1-298. DR PDB; 3R73; X-ray; 1.70 A; A=1-298. DR PDB; 3R7E; X-ray; 1.90 A; A=1-298. DR PDB; 3R7I; X-ray; 1.85 A; A=1-298. DR PDB; 3R7U; X-ray; 1.75 A; A=1-298. DR PDB; 3R7V; X-ray; 1.95 A; A=1-298. DR PDB; 3R7Y; X-ray; 1.90 A; A=1-298. DR PDB; 3R83; X-ray; 1.75 A; A=1-298. DR PDB; 3R8L; X-ray; 1.90 A; A=1-298. DR PDB; 3R8M; X-ray; 1.80 A; A=1-298. DR PDB; 3R8P; X-ray; 1.80 A; A=1-298. DR PDB; 3R8U; X-ray; 2.00 A; A=1-298. DR PDB; 3R8V; X-ray; 1.90 A; A=1-298. DR PDB; 3R8Z; X-ray; 1.85 A; A=1-298. DR PDB; 3R9D; X-ray; 1.95 A; A=1-298. DR PDB; 3R9H; X-ray; 2.10 A; A=1-298. DR PDB; 3R9N; X-ray; 1.75 A; A=1-298. DR PDB; 3R9O; X-ray; 1.90 A; A=1-298. DR PDB; 3RAH; X-ray; 1.75 A; A=1-298. DR PDB; 3RAI; X-ray; 1.70 A; A=1-298. DR PDB; 3RAK; X-ray; 1.75 A; A=1-298. DR PDB; 3RAL; X-ray; 1.75 A; A=1-298. DR PDB; 3RJC; X-ray; 1.85 A; A=1-298. DR PDB; 3RK5; X-ray; 2.00 A; A=1-298. DR PDB; 3RK7; X-ray; 1.80 A; A=1-298. DR PDB; 3RK9; X-ray; 1.85 A; A=1-298. DR PDB; 3RKB; X-ray; 2.00 A; A=1-298. DR PDB; 3RM6; X-ray; 1.60 A; A=1-298. DR PDB; 3RM7; X-ray; 1.85 A; A=1-298. DR PDB; 3RMF; X-ray; 1.75 A; A=1-298. DR PDB; 3RNI; X-ray; 1.95 A; A=1-298. DR PDB; 3ROY; X-ray; 1.75 A; A=1-298. DR PDB; 3RPO; X-ray; 1.75 A; A=1-298. DR PDB; 3RPR; X-ray; 1.75 A; A=1-298. DR PDB; 3RPV; X-ray; 1.80 A; A=1-298. DR PDB; 3RPY; X-ray; 1.90 A; A=1-298. DR PDB; 3RZB; X-ray; 1.90 A; A=1-298. DR PDB; 3S00; X-ray; 1.80 A; A=1-298. DR PDB; 3S0O; X-ray; 2.00 A; A=1-298. DR PDB; 3S1H; X-ray; 1.75 A; A=1-298. DR PDB; 3S2P; X-ray; 2.30 A; A=1-298. DR PDB; 3SQQ; X-ray; 1.85 A; A=1-298. DR PDB; 3SW4; X-ray; 1.70 A; A=1-298. DR PDB; 3SW7; X-ray; 1.80 A; A=1-298. DR PDB; 3TI1; X-ray; 1.99 A; A=1-298. DR PDB; 3TIY; X-ray; 1.84 A; A=1-298. DR PDB; 3TIZ; X-ray; 2.02 A; A=1-298. DR PDB; 3TNW; X-ray; 2.00 A; A/C=1-298. DR PDB; 3ULI; X-ray; 2.00 A; A=1-298. DR PDB; 3UNJ; X-ray; 1.90 A; A=1-298. DR PDB; 3UNK; X-ray; 2.10 A; A=1-298. DR PDB; 3WBL; X-ray; 2.00 A; A=1-298. DR PDB; 4ACM; X-ray; 1.63 A; A=1-298. DR PDB; 4BCK; X-ray; 2.05 A; A/C=1-298. DR PDB; 4BCM; X-ray; 2.45 A; A/C=1-298. DR PDB; 4BCN; X-ray; 2.10 A; A/C=1-298. DR PDB; 4BCO; X-ray; 2.05 A; A/C=1-298. DR PDB; 4BCP; X-ray; 2.26 A; A/C=1-298. DR PDB; 4BCQ; X-ray; 2.40 A; A/C=1-298. DR PDB; 4BGH; X-ray; 1.95 A; A=1-298. DR PDB; 4BZD; X-ray; 1.83 A; A=1-298. DR PDB; 4CFM; X-ray; 2.85 A; A/C=1-298. DR PDB; 4CFN; X-ray; 2.20 A; A/C=1-298. DR PDB; 4CFU; X-ray; 2.20 A; A/C=1-298. DR PDB; 4CFV; X-ray; 2.00 A; A/C=1-298. DR PDB; 4CFW; X-ray; 2.45 A; A/C=1-298. DR PDB; 4CFX; X-ray; 3.50 A; A/C=1-298. DR PDB; 4D1X; X-ray; 2.10 A; A=1-298. DR PDB; 4D1Z; X-ray; 1.85 A; A=1-298. DR PDB; 4EK3; X-ray; 1.34 A; A=1-298. DR PDB; 4EK4; X-ray; 1.26 A; A=1-298. DR PDB; 4EK5; X-ray; 1.60 A; A=1-298. DR PDB; 4EK6; X-ray; 1.52 A; A=1-298. DR PDB; 4EK8; X-ray; 1.70 A; A=1-298. DR PDB; 4EOI; X-ray; 2.00 A; A/C=1-298. DR PDB; 4EOJ; X-ray; 1.65 A; A/C=1-298. DR PDB; 4EOK; X-ray; 2.57 A; A/C=1-297. DR PDB; 4EOL; X-ray; 2.40 A; A/C=1-297. DR PDB; 4EOM; X-ray; 2.10 A; A/C=1-297. DR PDB; 4EON; X-ray; 2.40 A; A/C=1-298. DR PDB; 4EOO; X-ray; 2.10 A; A/C=1-297. DR PDB; 4EOP; X-ray; 1.99 A; A/C=1-297. DR PDB; 4EOQ; X-ray; 2.15 A; A/C=1-297. DR PDB; 4EOR; X-ray; 2.20 A; A/C=1-297. DR PDB; 4EOS; X-ray; 2.57 A; A/C=1-297. DR PDB; 4ERW; X-ray; 2.00 A; A=1-298. DR PDB; 4EZ3; X-ray; 2.00 A; A=1-298. DR PDB; 4EZ7; X-ray; 2.49 A; A=1-298. DR PDB; 4FKG; X-ray; 1.51 A; A=1-298. DR PDB; 4FKI; X-ray; 1.60 A; A=1-298. DR PDB; 4FKJ; X-ray; 1.63 A; A=1-298. DR PDB; 4FKL; X-ray; 1.26 A; A=1-298. DR PDB; 4FKO; X-ray; 1.55 A; A=1-298. DR PDB; 4FKP; X-ray; 1.60 A; A=1-298. DR PDB; 4FKQ; X-ray; 1.75 A; A=1-298. DR PDB; 4FKR; X-ray; 1.90 A; A=1-298. DR PDB; 4FKS; X-ray; 1.55 A; A=1-298. DR PDB; 4FKT; X-ray; 1.60 A; A=1-298. DR PDB; 4FKU; X-ray; 1.47 A; A=1-298. DR PDB; 4FKV; X-ray; 1.70 A; A=1-298. DR PDB; 4FKW; X-ray; 1.80 A; A=1-298. DR PDB; 4FX3; X-ray; 2.75 A; A/C=1-298. DR PDB; 4GCJ; X-ray; 1.42 A; A=1-298. DR PDB; 4I3Z; X-ray; 2.05 A; A/C=1-296. DR PDB; 4II5; X-ray; 2.15 A; A/C=1-298. DR PDB; 4KD1; X-ray; 1.70 A; A=1-298. DR PDB; 4LYN; X-ray; 2.00 A; A=1-298. DR PDB; 4NJ3; X-ray; 1.85 A; A=1-298. DR PDB; 4RJ3; X-ray; 1.63 A; A=1-298. DR PDB; 5A14; X-ray; 2.00 A; A=1-298. DR PDB; 5AND; X-ray; 2.30 A; A=1-298. DR PDB; 5ANE; X-ray; 1.70 A; A=1-298. DR PDB; 5ANG; X-ray; 1.90 A; A=1-298. DR PDB; 5ANI; X-ray; 1.90 A; A=1-298. DR PDB; 5ANJ; X-ray; 1.60 A; A=1-298. DR PDB; 5ANK; X-ray; 1.90 A; A=1-298. DR PDB; 5ANO; X-ray; 1.70 A; A=1-298. DR PDB; 5CYI; X-ray; 2.00 A; A/C=1-298. DR PDB; 5D1J; X-ray; 1.80 A; A=1-298. DR PDB; 5FP5; X-ray; 2.16 A; A=1-298. DR PDB; 5FP6; X-ray; 1.85 A; A=1-298. DR PDB; 5IEV; X-ray; 2.03 A; A=1-298. DR PDB; 5IEX; X-ray; 2.03 A; A=1-298. DR PDB; 5IEY; X-ray; 1.66 A; A=1-298. DR PDB; 5IF1; X-ray; 2.61 A; A/C=1-298. DR PDB; 5JQ5; X-ray; 1.94 A; A=1-298. DR PDB; 5JQ8; X-ray; 1.94 A; A=1-298. DR PDB; 5K4J; X-ray; 1.60 A; A=1-298. DR PDB; 5L2W; X-ray; 2.80 A; A=1-298. DR PDB; 5LMK; X-ray; 2.40 A; A=1-298, C=1-296. DR PDB; 5MHQ; X-ray; 1.30 A; A=1-298. DR PDB; 5NEV; X-ray; 2.97 A; A/C=1-298. DR PDB; 5OO0; X-ray; 1.60 A; A=1-298. DR PDB; 5OO1; X-ray; 2.00 A; A=1-298. DR PDB; 5OO3; X-ray; 1.73 A; A=1-298. DR PDB; 5OSJ; X-ray; 1.83 A; A=1-298. DR PDB; 5OSM; X-ray; 1.77 A; A=1-298. DR PDB; 5UQ1; X-ray; 3.20 A; A/C=1-298. DR PDB; 5UQ2; X-ray; 2.70 A; A=1-298. DR PDB; 5UQ3; X-ray; 3.60 A; A=1-298. DR PDB; 6ATH; X-ray; 1.82 A; A=1-298. DR PDB; 6GUB; X-ray; 2.52 A; A/C=1-298. DR PDB; 6GUC; X-ray; 2.00 A; A/C=1-298. DR PDB; 6GUE; X-ray; 1.99 A; A/C=1-298. DR PDB; 6GUF; X-ray; 2.65 A; A/C=1-298. DR PDB; 6GUH; X-ray; 1.50 A; A=1-298. DR PDB; 6GUK; X-ray; 1.30 A; A=1-298. DR PDB; 6GVA; X-ray; 2.15 A; A=1-298. DR PDB; 6INL; X-ray; 1.75 A; A=1-298. DR PDB; 6JGM; X-ray; 2.30 A; A=1-298. DR PDB; 6OQI; X-ray; 2.00 A; A=1-298. DR PDB; 6P3W; X-ray; 2.54 A; A/C=1-298. DR PDB; 6Q3B; X-ray; 1.11 A; A=1-298. DR PDB; 6Q3C; X-ray; 1.29 A; A=1-298. DR PDB; 6Q3F; X-ray; 1.18 A; A=1-298. DR PDB; 6Q48; X-ray; 1.03 A; A=1-298. DR PDB; 6Q49; X-ray; 1.00 A; A=1-298. DR PDB; 6Q4A; X-ray; 1.13 A; A=1-298. DR PDB; 6Q4B; X-ray; 1.12 A; A=1-298. DR PDB; 6Q4C; X-ray; 1.73 A; A=1-298. DR PDB; 6Q4D; X-ray; 1.07 A; A=1-298. DR PDB; 6Q4E; X-ray; 1.06 A; A=1-298. DR PDB; 6Q4F; X-ray; 1.21 A; A=1-298. DR PDB; 6Q4G; X-ray; 0.98 A; A=1-298. DR PDB; 6Q4H; X-ray; 1.00 A; A=1-298. DR PDB; 6Q4I; X-ray; 1.11 A; A=1-298. DR PDB; 6Q4J; X-ray; 1.05 A; A=1-298. DR PDB; 6Q4K; X-ray; 1.06 A; A=1-298. DR PDB; 6RIJ; X-ray; 2.20 A; A/C=1-298. DR PDB; 6SG4; X-ray; 2.43 A; A/C=1-298. DR PDB; 6YL1; X-ray; 1.66 A; A=1-298. DR PDB; 6YL6; X-ray; 1.70 A; A=1-298. DR PDB; 6YLK; X-ray; 1.65 A; A=1-298. DR PDB; 7ACK; X-ray; 1.80 A; A/C=1-298. DR PDB; 7B5L; EM; 3.80 A; L=1-298. DR PDB; 7B5R; EM; 3.80 A; L=1-298. DR PDB; 7B7S; X-ray; 2.54 A; A/C=1-298. DR PDB; 7E34; X-ray; 3.19 A; A=2-298. DR PDB; 7KJS; X-ray; 2.19 A; A=1-298. DR PDB; 7M2F; X-ray; 1.63 A; A=1-298. DR PDB; 7MKX; X-ray; 3.08 A; A/C=1-298. DR PDB; 7NVQ; X-ray; 2.05 A; A=1-298. DR PDB; 7QHL; X-ray; 1.70 A; A/C=1-298. DR PDB; 7RA5; X-ray; 1.67 A; A=1-298. DR PDB; 7RWE; X-ray; 1.59 A; A=1-298. DR PDB; 7RWF; X-ray; 1.50 A; A=1-298. DR PDB; 7RXO; X-ray; 1.38 A; A=1-298. DR PDB; 7S4T; X-ray; 1.91 A; A=1-298. DR PDB; 7S7A; X-ray; 1.70 A; A=1-298. DR PDB; 7S84; X-ray; 2.00 A; A=1-298. DR PDB; 7S85; X-ray; 1.98 A; A=1-298. DR PDB; 7S9X; X-ray; 1.69 A; A=1-298. DR PDB; 7SA0; X-ray; 1.59 A; A=1-298. DR PDB; 7UG1; X-ray; 1.84 A; A=1-298. DR PDB; 7UXI; X-ray; 2.07 A; A=1-298. DR PDB; 7UXK; X-ray; 2.63 A; A=1-298. DR PDB; 7VDU; X-ray; 1.53 A; A=1-298. DR PDB; 7ZPC; X-ray; 1.40 A; A=1-298. DR PDB; 8B54; X-ray; 2.60 A; A/C=1-298. DR PDB; 8BYA; EM; 3.38 A; A=1-298. DR PDB; 8BZO; EM; 3.50 A; A=1-297. DR PDB; 8CUR; X-ray; 2.20 A; A=1-298. DR PDB; 8ERD; X-ray; 1.33 A; A=1-298. DR PDB; 8ERN; X-ray; 1.64 A; A=1-298. DR PDB; 8FOW; X-ray; 1.60 A; A=1-298. DR PDB; 8FP0; X-ray; 1.60 A; A=1-298. DR PDB; 8FP5; X-ray; 1.70 A; A=1-298. DR PDB; 8H6P; X-ray; 2.44 A; A=1-297. DR PDB; 8H6T; X-ray; 3.00 A; A=1-297. DR PDB; 8OR0; EM; 3.10 A; H=1-298. DR PDB; 8OR4; EM; 3.80 A; H=1-298. DR PDB; 8OY2; X-ray; 2.62 A; A=1-298. DR PDBsum; 1AQ1; -. DR PDBsum; 1B38; -. DR PDBsum; 1B39; -. DR PDBsum; 1BUH; -. DR PDBsum; 1CKP; -. DR PDBsum; 1DI8; -. DR PDBsum; 1DM2; -. DR PDBsum; 1E1V; -. DR PDBsum; 1E1X; -. DR PDBsum; 1E9H; -. DR PDBsum; 1F5Q; -. DR PDBsum; 1FIN; -. DR PDBsum; 1FQ1; -. DR PDBsum; 1FVT; -. DR PDBsum; 1FVV; -. DR PDBsum; 1G5S; -. DR PDBsum; 1GIH; -. DR PDBsum; 1GII; -. DR PDBsum; 1GIJ; -. DR PDBsum; 1GY3; -. DR PDBsum; 1GZ8; -. DR PDBsum; 1H00; -. DR PDBsum; 1H01; -. DR PDBsum; 1H07; -. DR PDBsum; 1H08; -. DR PDBsum; 1H0V; -. DR PDBsum; 1H0W; -. DR PDBsum; 1H1P; -. DR PDBsum; 1H1Q; -. DR PDBsum; 1H1R; -. DR PDBsum; 1H1S; -. DR PDBsum; 1H24; -. DR PDBsum; 1H25; -. DR PDBsum; 1H26; -. DR PDBsum; 1H27; -. DR PDBsum; 1H28; -. DR PDBsum; 1HCK; -. DR PDBsum; 1HCL; -. DR PDBsum; 1JST; -. DR PDBsum; 1JSU; -. DR PDBsum; 1JSV; -. DR PDBsum; 1JVP; -. DR PDBsum; 1KE5; -. DR PDBsum; 1KE6; -. DR PDBsum; 1KE7; -. DR PDBsum; 1KE8; -. DR PDBsum; 1KE9; -. DR PDBsum; 1OGU; -. DR PDBsum; 1OI9; -. DR PDBsum; 1OIQ; -. DR PDBsum; 1OIR; -. DR PDBsum; 1OIT; -. DR PDBsum; 1OIU; -. DR PDBsum; 1OIY; -. DR PDBsum; 1OKV; -. DR PDBsum; 1OKW; -. DR PDBsum; 1OL1; -. DR PDBsum; 1OL2; -. DR PDBsum; 1P2A; -. DR PDBsum; 1P5E; -. DR PDBsum; 1PF8; -. DR PDBsum; 1PKD; -. DR PDBsum; 1PW2; -. DR PDBsum; 1PXI; -. DR PDBsum; 1PXJ; -. DR PDBsum; 1PXK; -. DR PDBsum; 1PXL; -. DR PDBsum; 1PXM; -. DR PDBsum; 1PXN; -. DR PDBsum; 1PXO; -. DR PDBsum; 1PXP; -. DR PDBsum; 1PYE; -. DR PDBsum; 1QMZ; -. DR PDBsum; 1R78; -. DR PDBsum; 1URC; -. DR PDBsum; 1URW; -. DR PDBsum; 1V1K; -. DR PDBsum; 1VYW; -. DR PDBsum; 1VYZ; -. DR PDBsum; 1W0X; -. DR PDBsum; 1W8C; -. DR PDBsum; 1W98; -. DR PDBsum; 1WCC; -. DR PDBsum; 1Y8Y; -. DR PDBsum; 1Y91; -. DR PDBsum; 1YKR; -. DR PDBsum; 2A0C; -. DR PDBsum; 2A4L; -. DR PDBsum; 2B52; -. DR PDBsum; 2B53; -. DR PDBsum; 2B54; -. DR PDBsum; 2B55; -. DR PDBsum; 2BHE; -. DR PDBsum; 2BHH; -. DR PDBsum; 2BKZ; -. DR PDBsum; 2BPM; -. DR PDBsum; 2BTR; -. DR PDBsum; 2BTS; -. DR PDBsum; 2C4G; -. DR PDBsum; 2C5N; -. DR PDBsum; 2C5O; -. DR PDBsum; 2C5V; -. DR PDBsum; 2C5X; -. DR PDBsum; 2C5Y; -. DR PDBsum; 2C68; -. DR PDBsum; 2C69; -. DR PDBsum; 2C6I; -. DR PDBsum; 2C6K; -. DR PDBsum; 2C6L; -. DR PDBsum; 2C6M; -. DR PDBsum; 2C6O; -. DR PDBsum; 2C6T; -. DR PDBsum; 2CCH; -. DR PDBsum; 2CCI; -. DR PDBsum; 2CJM; -. DR PDBsum; 2CLX; -. DR PDBsum; 2DS1; -. DR PDBsum; 2DUV; -. DR PDBsum; 2EXM; -. DR PDBsum; 2FVD; -. DR PDBsum; 2G9X; -. DR PDBsum; 2I40; -. DR PDBsum; 2IW6; -. DR PDBsum; 2IW8; -. DR PDBsum; 2IW9; -. DR PDBsum; 2J9M; -. DR PDBsum; 2JGZ; -. DR PDBsum; 2R3F; -. DR PDBsum; 2R3G; -. DR PDBsum; 2R3H; -. DR PDBsum; 2R3I; -. DR PDBsum; 2R3J; -. DR PDBsum; 2R3K; -. DR PDBsum; 2R3L; -. DR PDBsum; 2R3M; -. DR PDBsum; 2R3N; -. DR PDBsum; 2R3O; -. DR PDBsum; 2R3P; -. DR PDBsum; 2R3Q; -. DR PDBsum; 2R3R; -. DR PDBsum; 2R64; -. DR PDBsum; 2UUE; -. DR PDBsum; 2UZB; -. DR PDBsum; 2UZD; -. DR PDBsum; 2UZE; -. DR PDBsum; 2UZL; -. DR PDBsum; 2UZN; -. DR PDBsum; 2UZO; -. DR PDBsum; 2V0D; -. DR PDBsum; 2V22; -. DR PDBsum; 2VTA; -. DR PDBsum; 2VTH; -. DR PDBsum; 2VTI; -. DR PDBsum; 2VTJ; -. DR PDBsum; 2VTL; -. DR PDBsum; 2VTM; -. DR PDBsum; 2VTN; -. DR PDBsum; 2VTO; -. DR PDBsum; 2VTP; -. DR PDBsum; 2VTQ; -. DR PDBsum; 2VTR; -. DR PDBsum; 2VTS; -. DR PDBsum; 2VTT; -. DR PDBsum; 2VU3; -. DR PDBsum; 2VV9; -. DR PDBsum; 2W05; -. DR PDBsum; 2W06; -. DR PDBsum; 2W17; -. DR PDBsum; 2W1H; -. DR PDBsum; 2WEV; -. DR PDBsum; 2WFY; -. DR PDBsum; 2WHB; -. DR PDBsum; 2WIH; -. DR PDBsum; 2WIP; -. DR PDBsum; 2WMA; -. DR PDBsum; 2WMB; -. DR PDBsum; 2WPA; -. DR PDBsum; 2WXV; -. DR PDBsum; 2X1N; -. DR PDBsum; 2XMY; -. DR PDBsum; 2XNB; -. DR PDBsum; 3BHT; -. DR PDBsum; 3BHU; -. DR PDBsum; 3BHV; -. DR PDBsum; 3DDP; -. DR PDBsum; 3DDQ; -. DR PDBsum; 3DOG; -. DR PDBsum; 3EID; -. DR PDBsum; 3EJ1; -. DR PDBsum; 3EOC; -. DR PDBsum; 3EZR; -. DR PDBsum; 3EZV; -. DR PDBsum; 3F5X; -. DR PDBsum; 3FZ1; -. DR PDBsum; 3IG7; -. DR PDBsum; 3IGG; -. DR PDBsum; 3LE6; -. DR PDBsum; 3LFN; -. DR PDBsum; 3LFQ; -. DR PDBsum; 3LFS; -. DR PDBsum; 3MY5; -. DR PDBsum; 3NS9; -. DR PDBsum; 3PJ8; -. DR PDBsum; 3PXF; -. DR PDBsum; 3PXQ; -. DR PDBsum; 3PXR; -. DR PDBsum; 3PXY; -. DR PDBsum; 3PXZ; -. DR PDBsum; 3PY0; -. DR PDBsum; 3PY1; -. DR PDBsum; 3QHR; -. DR PDBsum; 3QHW; -. DR PDBsum; 3QL8; -. DR PDBsum; 3QQF; -. DR PDBsum; 3QQG; -. DR PDBsum; 3QQH; -. DR PDBsum; 3QQJ; -. DR PDBsum; 3QQK; -. DR PDBsum; 3QQL; -. DR PDBsum; 3QRT; -. DR PDBsum; 3QRU; -. DR PDBsum; 3QTQ; -. DR PDBsum; 3QTR; -. DR PDBsum; 3QTS; -. DR PDBsum; 3QTU; -. DR PDBsum; 3QTW; -. DR PDBsum; 3QTX; -. DR PDBsum; 3QTZ; -. DR PDBsum; 3QU0; -. DR PDBsum; 3QWJ; -. DR PDBsum; 3QWK; -. DR PDBsum; 3QX2; -. DR PDBsum; 3QX4; -. DR PDBsum; 3QXO; -. DR PDBsum; 3QXP; -. DR PDBsum; 3QZF; -. DR PDBsum; 3QZG; -. DR PDBsum; 3QZH; -. DR PDBsum; 3QZI; -. DR PDBsum; 3R1Q; -. DR PDBsum; 3R1S; -. DR PDBsum; 3R1Y; -. DR PDBsum; 3R28; -. DR PDBsum; 3R6X; -. DR PDBsum; 3R71; -. DR PDBsum; 3R73; -. DR PDBsum; 3R7E; -. DR PDBsum; 3R7I; -. DR PDBsum; 3R7U; -. DR PDBsum; 3R7V; -. DR PDBsum; 3R7Y; -. DR PDBsum; 3R83; -. DR PDBsum; 3R8L; -. DR PDBsum; 3R8M; -. DR PDBsum; 3R8P; -. DR PDBsum; 3R8U; -. DR PDBsum; 3R8V; -. DR PDBsum; 3R8Z; -. DR PDBsum; 3R9D; -. DR PDBsum; 3R9H; -. DR PDBsum; 3R9N; -. DR PDBsum; 3R9O; -. DR PDBsum; 3RAH; -. DR PDBsum; 3RAI; -. DR PDBsum; 3RAK; -. DR PDBsum; 3RAL; -. DR PDBsum; 3RJC; -. DR PDBsum; 3RK5; -. DR PDBsum; 3RK7; -. DR PDBsum; 3RK9; -. DR PDBsum; 3RKB; -. DR PDBsum; 3RM6; -. DR PDBsum; 3RM7; -. DR PDBsum; 3RMF; -. DR PDBsum; 3RNI; -. DR PDBsum; 3ROY; -. DR PDBsum; 3RPO; -. DR PDBsum; 3RPR; -. DR PDBsum; 3RPV; -. DR PDBsum; 3RPY; -. DR PDBsum; 3RZB; -. DR PDBsum; 3S00; -. DR PDBsum; 3S0O; -. DR PDBsum; 3S1H; -. DR PDBsum; 3S2P; -. DR PDBsum; 3SQQ; -. DR PDBsum; 3SW4; -. DR PDBsum; 3SW7; -. DR PDBsum; 3TI1; -. DR PDBsum; 3TIY; -. DR PDBsum; 3TIZ; -. DR PDBsum; 3TNW; -. DR PDBsum; 3ULI; -. DR PDBsum; 3UNJ; -. DR PDBsum; 3UNK; -. DR PDBsum; 3WBL; -. DR PDBsum; 4ACM; -. DR PDBsum; 4BCK; -. DR PDBsum; 4BCM; -. DR PDBsum; 4BCN; -. DR PDBsum; 4BCO; -. DR PDBsum; 4BCP; -. DR PDBsum; 4BCQ; -. DR PDBsum; 4BGH; -. DR PDBsum; 4BZD; -. DR PDBsum; 4CFM; -. DR PDBsum; 4CFN; -. DR PDBsum; 4CFU; -. DR PDBsum; 4CFV; -. DR PDBsum; 4CFW; -. DR PDBsum; 4CFX; -. DR PDBsum; 4D1X; -. DR PDBsum; 4D1Z; -. DR PDBsum; 4EK3; -. DR PDBsum; 4EK4; -. DR PDBsum; 4EK5; -. DR PDBsum; 4EK6; -. DR PDBsum; 4EK8; -. DR PDBsum; 4EOI; -. DR PDBsum; 4EOJ; -. DR PDBsum; 4EOK; -. DR PDBsum; 4EOL; -. DR PDBsum; 4EOM; -. DR PDBsum; 4EON; -. DR PDBsum; 4EOO; -. DR PDBsum; 4EOP; -. DR PDBsum; 4EOQ; -. DR PDBsum; 4EOR; -. DR PDBsum; 4EOS; -. DR PDBsum; 4ERW; -. DR PDBsum; 4EZ3; -. DR PDBsum; 4EZ7; -. DR PDBsum; 4FKG; -. DR PDBsum; 4FKI; -. DR PDBsum; 4FKJ; -. DR PDBsum; 4FKL; -. DR PDBsum; 4FKO; -. DR PDBsum; 4FKP; -. DR PDBsum; 4FKQ; -. DR PDBsum; 4FKR; -. DR PDBsum; 4FKS; -. DR PDBsum; 4FKT; -. DR PDBsum; 4FKU; -. DR PDBsum; 4FKV; -. DR PDBsum; 4FKW; -. DR PDBsum; 4FX3; -. DR PDBsum; 4GCJ; -. DR PDBsum; 4I3Z; -. DR PDBsum; 4II5; -. DR PDBsum; 4KD1; -. DR PDBsum; 4LYN; -. DR PDBsum; 4NJ3; -. DR PDBsum; 4RJ3; -. DR PDBsum; 5A14; -. DR PDBsum; 5AND; -. DR PDBsum; 5ANE; -. DR PDBsum; 5ANG; -. DR PDBsum; 5ANI; -. DR PDBsum; 5ANJ; -. DR PDBsum; 5ANK; -. DR PDBsum; 5ANO; -. DR PDBsum; 5CYI; -. DR PDBsum; 5D1J; -. DR PDBsum; 5FP5; -. DR PDBsum; 5FP6; -. DR PDBsum; 5IEV; -. DR PDBsum; 5IEX; -. DR PDBsum; 5IEY; -. DR PDBsum; 5IF1; -. DR PDBsum; 5JQ5; -. DR PDBsum; 5JQ8; -. DR PDBsum; 5K4J; -. DR PDBsum; 5L2W; -. DR PDBsum; 5LMK; -. DR PDBsum; 5MHQ; -. DR PDBsum; 5NEV; -. DR PDBsum; 5OO0; -. DR PDBsum; 5OO1; -. DR PDBsum; 5OO3; -. DR PDBsum; 5OSJ; -. DR PDBsum; 5OSM; -. DR PDBsum; 5UQ1; -. DR PDBsum; 5UQ2; -. DR PDBsum; 5UQ3; -. DR PDBsum; 6ATH; -. DR PDBsum; 6GUB; -. DR PDBsum; 6GUC; -. DR PDBsum; 6GUE; -. DR PDBsum; 6GUF; -. DR PDBsum; 6GUH; -. DR PDBsum; 6GUK; -. DR PDBsum; 6GVA; -. DR PDBsum; 6INL; -. DR PDBsum; 6JGM; -. DR PDBsum; 6OQI; -. DR PDBsum; 6P3W; -. DR PDBsum; 6Q3B; -. DR PDBsum; 6Q3C; -. DR PDBsum; 6Q3F; -. DR PDBsum; 6Q48; -. DR PDBsum; 6Q49; -. DR PDBsum; 6Q4A; -. DR PDBsum; 6Q4B; -. DR PDBsum; 6Q4C; -. DR PDBsum; 6Q4D; -. DR PDBsum; 6Q4E; -. DR PDBsum; 6Q4F; -. DR PDBsum; 6Q4G; -. DR PDBsum; 6Q4H; -. DR PDBsum; 6Q4I; -. DR PDBsum; 6Q4J; -. DR PDBsum; 6Q4K; -. DR PDBsum; 6RIJ; -. DR PDBsum; 6SG4; -. DR PDBsum; 6YL1; -. DR PDBsum; 6YL6; -. DR PDBsum; 6YLK; -. DR PDBsum; 7ACK; -. DR PDBsum; 7B5L; -. DR PDBsum; 7B5R; -. DR PDBsum; 7B7S; -. DR PDBsum; 7E34; -. DR PDBsum; 7KJS; -. DR PDBsum; 7M2F; -. DR PDBsum; 7MKX; -. DR PDBsum; 7NVQ; -. DR PDBsum; 7QHL; -. DR PDBsum; 7RA5; -. DR PDBsum; 7RWE; -. DR PDBsum; 7RWF; -. DR PDBsum; 7RXO; -. DR PDBsum; 7S4T; -. DR PDBsum; 7S7A; -. DR PDBsum; 7S84; -. DR PDBsum; 7S85; -. DR PDBsum; 7S9X; -. DR PDBsum; 7SA0; -. DR PDBsum; 7UG1; -. DR PDBsum; 7UXI; -. DR PDBsum; 7UXK; -. DR PDBsum; 7VDU; -. DR PDBsum; 7ZPC; -. DR PDBsum; 8B54; -. DR PDBsum; 8BYA; -. DR PDBsum; 8BZO; -. DR PDBsum; 8CUR; -. DR PDBsum; 8ERD; -. DR PDBsum; 8ERN; -. DR PDBsum; 8FOW; -. DR PDBsum; 8FP0; -. DR PDBsum; 8FP5; -. DR PDBsum; 8H6P; -. DR PDBsum; 8H6T; -. DR PDBsum; 8OR0; -. DR PDBsum; 8OR4; -. DR PDBsum; 8OY2; -. DR AlphaFoldDB; P24941; -. DR EMDB; EMD-12037; -. DR EMDB; EMD-12048; -. DR EMDB; EMD-16325; -. DR EMDB; EMD-16344; -. DR EMDB; EMD-17114; -. DR EMDB; EMD-17117; -. DR EMDB; EMD-4467; -. DR SMR; P24941; -. DR BioGRID; 107452; 797. DR ComplexPortal; CPX-2005; Cyclin A1-CDK2 complex. DR ComplexPortal; CPX-2006; Cyclin A2-CDK2 complex. DR ComplexPortal; CPX-2009; Cyclin B3-CDK2 complex. DR ComplexPortal; CPX-2015; Cyclin E1-CDK2 complex. DR ComplexPortal; CPX-2016; Cyclin E2-CDK2 complex. DR CORUM; P24941; -. DR DIP; DIP-161N; -. DR ELM; P24941; -. DR IntAct; P24941; 186. DR MINT; P24941; -. DR STRING; 9606.ENSP00000266970; -. DR BindingDB; P24941; -. DR ChEMBL; CHEMBL301; -. DR DrugBank; DB06888; (13R,15S)-13-METHYL-16-OXA-8,9,12,22,24-PENTAAZAHEXACYCLO[15.6.2.16,9.1,12,15.0,2,7.0,21,25]HEPTACOSA-1(24),2,4,6,17(25),18,20-HEPTAENE-23,26-DIONE. DR DrugBank; DB03583; (2E,3S)-3-hydroxy-5'-[(4-hydroxypiperidin-1-yl)sulfonyl]-3-methyl-1,3-dihydro-2,3'-biindol-2'(1'H)-one. DR DrugBank; DB07054; (2R)-1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENOXY}PROPAN-2-OL. DR DrugBank; DB07750; (2R)-1-[4-({4-[(2,5-Dichlorophenyl)amino]-2-pyrimidinyl}amino)phenoxy]-3-(dimethylamino)-2-propanol. DR DrugBank; DB07761; (2R)-1-[4-({6-[(2,6-Difluorophenyl)amino]-4-pyrimidinyl}amino)phenoxy]-3-(dimethylamino)-2-propanol. DR DrugBank; DB07504; (2R)-1-{4-[(4-Anilino-5-bromo-2-pyrimidinyl)amino]phenoxy}-3-(dimethylamino)-2-propanol. DR DrugBank; DB08463; (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol. DR DrugBank; DB08285; (2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol. DR DrugBank; DB07889; (2S)-1-(Dimethylamino)-3-(4-{[4-(2-methylimidazo[1,2-a]pyridin-3-yl)-2-pyrimidinyl]amino}phenoxy)-2-propanol. DR DrugBank; DB07755; (2S)-1-[4-({4-[(2,5-Dichlorophenyl)amino]-2-pyrimidinyl}amino)phenoxy]-3-(dimethylamino)-2-propanol. DR DrugBank; DB07751; (2S)-1-[4-({6-[(2,6-Difluorophenyl)amino]-4-pyrimidinyl}amino)phenoxy]-3-(dimethylamino)-2-propanol. DR DrugBank; DB07501; (2S)-1-{4-[(4-Anilino-5-bromo-2-pyrimidinyl)amino]phenoxy}-3-(dimethylamino)-2-propanol. DR DrugBank; DB07137; (2S)-N-[(3E)-5-Cyclopropyl-3H-pyrazol-3-ylidene]-2-[4-(2-oxo-1-imidazolidinyl)phenyl]propanamide. DR DrugBank; DB07431; (3R)-3-(aminomethyl)-9-methoxy-1,2,3,4-tetrahydro-5H-[1]benzothieno[3,2-e][1,4]diazepin-5-one. DR DrugBank; DB08137; (4E)-N-(4-fluorophenyl)-4-[(phenylcarbonyl)imino]-4H-pyrazole-3-carboxamide. DR DrugBank; DB02963; (5-Chloropyrazolo[1,5-a]Pyrimidin-7-Yl)-(4-Methanesulfonylphenyl)Amine. DR DrugBank; DB06983; (5-phenyl-7-(pyridin-3-ylmethylamino)pyrazolo[1,5-a]pyrimidin-3-yl)methanol. DR DrugBank; DB07529; (5E)-2-Amino-5-(2-pyridinylmethylene)-1,3-thiazol-4(5H)-one. DR DrugBank; DB02898; (5R)-5-{[(2-Amino-3H-purin-6-yl)oxy]methyl}-2-pyrrolidinone. DR DrugBank; DB07595; (5Z)-5-(3-BROMOCYCLOHEXA-2,5-DIEN-1-YLIDENE)-N-(PYRIDIN-4-YLMETHYL)-1,5-DIHYDROPYRAZOLO[1,5-A]PYRIMIDIN-7-AMINE. DR DrugBank; DB07852; 1-(3,5-DICHLOROPHENYL)-5-METHYL-1H-1,2,4-TRIAZOLE-3-CARBOXYLIC ACID. DR DrugBank; DB07622; 1-(3-(2,4-DIMETHYLTHIAZOL-5-YL)-4-OXO-2,4-DIHYDROINDENO[1,2-C]PYRAZOL-5-YL)-3-(4-METHYLPIPERAZIN-1-YL)UREA. DR DrugBank; DB06976; 1-(5-OXO-2,3,5,9B-TETRAHYDRO-1H-PYRROLO[2,1-A]ISOINDOL-9-YL)-3-(5-PYRROLIDIN-2-YL-1H-PYRAZOL-3-YL)-UREA. DR DrugBank; DB03663; 1-[(2-Amino-6,9-Dihydro-1h-Purin-6-Yl)Oxy]-3-Methyl-2-Butanol. DR DrugBank; DB08527; 1-[4-(AMINOSULFONYL)PHENYL]-1,6-DIHYDROPYRAZOLO[3,4-E]INDAZOLE-3-CARBOXAMIDE. DR DrugBank; DB02603; 1-Amino-6-Cyclohex-3-Enylmethyloxypurine. DR DrugBank; DB08355; 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid. DR DrugBank; DB07024; 2-(3,4-DIHYDROXYPHENYL)-8-(1,1-DIOXIDOISOTHIAZOLIDIN-2-YL)-3-HYDROXY-6-METHYL-4H-CHROMEN-4-ONE. DR DrugBank; DB07618; 2-(4-(AMINOMETHYL)PIPERIDIN-1-YL)-N-(3_CYCLOHEXYL-4-OXO-2,4-DIHYDROINDENO[1,2-C]PYRAZOL-5-YL)ACETAMIDE. DR DrugBank; DB04288; 2-[Trans-(4-Aminocyclohexyl)Amino]-6-(Benzyl-Amino)-9-Cyclopentylpurine. DR DrugBank; DB02297; 2-Amino-6-Chloropyrazine. DR DrugBank; DB06948; 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE. DR DrugBank; DB07982; 2-{4-[4-({4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-yl}amino)phenyl]piperazin-1-yl}-2-oxoethanol. DR DrugBank; DB07179; 3-((3-bromo-5-o-tolylpyrazolo[1,5-a]pyrimidin-7-ylamino)methyl)pyridine 1-oxide. DR DrugBank; DB08248; 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE. DR DrugBank; DB08309; 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL. DR DrugBank; DB04518; 3-[4-(2,4-Dimethyl-Thiazol-5-Yl)-Pyrimidin-2-Ylamino]-Phenol. DR DrugBank; DB08535; 3-bromo-5-phenyl-N-(pyridin-3-ylmethyl)pyrazolo[1,5-a]pyrimidin-7-amine. DR DrugBank; DB07210; 3-bromo-5-phenyl-N-(pyridin-4-ylmethyl)pyrazolo[1,5-a]pyrimidin-7-amine. DR DrugBank; DB08536; 3-bromo-5-phenyl-N-(pyrimidin-5-ylmethyl)pyrazolo[1,5-a]pyridin-7-amine. DR DrugBank; DB08537; 3-bromo-6-phenyl-N-(pyrimidin-5-ylmethyl)imidazo[1,2-a]pyridin-8-amine. DR DrugBank; DB08539; 3-cyclopropyl-5-phenyl-N-(pyridin-3-ylmethyl)pyrazolo[1,5-a]pyrimidin-7-amine. DR DrugBank; DB08533; 3-methyl-N-(pyridin-4-ylmethyl)imidazo[1,2-a]pyrazin-8-amine. DR DrugBank; DB03490; 3-Pyridin-4-Yl-2,4-Dihydro-Indeno[1,2-.C.]Pyrazole. DR DrugBank; DB08124; 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. DR DrugBank; DB08126; 3-{[4-([amino(imino)methyl]aminosulfonyl)anilino]methylene}-2-oxo-2,3-dihydro-1H-indole. DR DrugBank; DB03737; 4-((3r,4s,5r)-4-Amino-3,5-Dihydroxy-Hex-1-Ynyl)-5-Fluoro-3-[1-(3-Methoxy-1h-Pyrrol-2-Yl)-Meth-(Z)-Ylidene]-1,3-Dihydro-Indol-2-One. DR DrugBank; DB02915; 4-(2,4-Dimethyl-1,3-thiazol-5-yl)-N-[4-(trifluoromethyl)phenyl]-2-pyrimidinamine. DR DrugBank; DB02091; 4-(2,4-Dimethyl-Thiazol-5-Yl)-Pyrimidin-2-Ylamine. DR DrugBank; DB03019; 4-(2,5-Dichloro-Thiophen-3-Yl)-Pyrimidin-2-Ylamine. DR DrugBank; DB08178; 4-(4-methoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine. DR DrugBank; DB08182; 4-(4-propoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine. DR DrugBank; DB02973; 4-(5-Bromo-2-Oxo-2h-Indol-3-Ylazo)-Benzenesulfonamide. DR DrugBank; DB08241; 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE. DR DrugBank; DB08136; 4-(acetylamino)-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamide. DR DrugBank; DB07687; 4-({5-[(4-AMINOCYCLOHEXYL)AMINO][1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL}AMINO)BENZENESULFONAMIDE. DR DrugBank; DB02197; 4-[(4-Imidazo[1,2-a]Pyridin-3-Ylpyrimidin-2-Yl)Amino]Benzenesulfonamide. DR DrugBank; DB08673; 4-[(5-ISOPROPYL-1,3-THIAZOL-2-YL)AMINO]BENZENESULFONAMIDE. DR DrugBank; DB03307; 4-[(6-Amino-4-Pyrimidinyl)Amino]Benzenesulfonamide. DR DrugBank; DB08134; 4-[(6-chloropyrazin-2-yl)amino]benzenesulfonamide. DR DrugBank; DB06844; 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE. DR DrugBank; DB03365; 4-[3-Hydroxyanilino]-6,7-Dimethoxyquinazoline. DR DrugBank; DB04407; 4-[4-(4-Methyl-2-Methylamino-Thiazol-5-Yl)-Pyrimidin-2-Ylamino]-Phenol. DR DrugBank; DB01888; 4-[5-(Trans-4-Aminocyclohexylamino)-3-Isopropylpyrazolo[1,5-a]Pyrimidin-7-Ylamino]-N,N-Dimethylbenzenesulfonamide. DR DrugBank; DB08219; 4-Methyl-5-[(2Z)-2-{[4-(4-morpholinyl)phenyl]imino}-2,5-dihydro-4-pyrimidinyl]-1,3-thiazol-2-amine. DR DrugBank; DB07540; 4-{5-[(1Z)-1-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)ETHYL]-2-FURYL}BENZENESULFONAMIDE. DR DrugBank; DB07531; 4-{5-[(Z)-(2,4-DIOXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZENESULFONAMIDE. DR DrugBank; DB07533; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]-2-FURYL}-N-METHYLBENZENESULFONAMIDE. DR DrugBank; DB07538; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}-2-(TRIFLUOROMETHYL)BENZENESULFONAMIDE. DR DrugBank; DB07534; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZENESULFONAMIDE. DR DrugBank; DB07539; 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZOIC ACID. DR DrugBank; DB08141; 4-{[(2,6-difluorophenyl)carbonyl]amino}-N-[(3S)-piperidin-3-yl]-1H-pyrazole-3-carboxamide. DR DrugBank; DB08125; 4-{[(2-Oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]amino}-N-(1,3-thiazol-2-yl)benzenesulfonamide. DR DrugBank; DB07791; 4-{[4-(1-CYCLOPROPYL-2-METHYL-1H-IMIDAZOL-5-YL)PYRIMIDIN-2-YL]AMINO}-N-METHYLBENZENESULFONAMIDE. DR DrugBank; DB08572; 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE. DR DrugBank; DB07686; 4-{[5-(CYCLOHEXYLAMINO)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE. DR DrugBank; DB07685; 4-{[5-(CYCLOHEXYLMETHOXY)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE. DR DrugBank; DB07688; 4-{[5-(CYCLOHEXYLOXY)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE. DR DrugBank; DB07065; 5-(2,3-dichlorophenyl)-N-(pyridin-4-ylmethyl)-3-thiocyanatopyrazolo[1,5-a]pyrimidin-7-amine. DR DrugBank; DB08531; 5-(2,3-dichlorophenyl)-N-(pyridin-4-ylmethyl)pyrazolo[1,5-a]pyrimidin-7-amine. DR DrugBank; DB08534; 5-(2-fluorophenyl)-N-(pyridin-4-ylmethyl)pyrazolo[1,5-a]pyrimidin-7-amine. DR DrugBank; DB07163; 5-[(2-AMINOETHYL)AMINO]-6-FLUORO-3-(1H-PYRROL-2-YL)BENZO[CD]INDOL-2(1H)-ONE. DR DrugBank; DB08140; 5-[(4-AMINOCYCLOHEXYL)AMINO]-7-(PROPAN-2-YLAMINO)PYRAZOLO[1,5-A]PYRIMIDINE-3-CARBONITRILE. DR DrugBank; DB07471; 5-[5,6-BIS(METHYLOXY)-1H-BENZIMIDAZOL-1-YL]-3-{[1-(2-CHLOROPHENYL)ETHYL]OXY}-2-THIOPHENECARBOXAMIDE. DR DrugBank; DB07493; 5-Bromoindirubin. DR DrugBank; DB08139; 5-chloro-7-[(1-methylethyl)amino]pyrazolo[1,5-a]pyrimidine-3-carbonitrile. DR DrugBank; DB08132; 5-hydroxynaphthalene-1-sulfonamide. DR DrugBank; DB08532; 6-(2-fluorophenyl)-N-(pyridin-3-ylmethyl)imidazo[1,2-a]pyrazin-8-amine. DR DrugBank; DB07606; 6-(3,4-DIHYDROXYBENZYL)-3-ETHYL-1-(2,4,6-TRICHLOROPHENYL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4(5H)-ONE. DR DrugBank; DB07612; 6-(3-AMINOPHENYL)-N-(TERT-BUTYL)-2-(TRIFLUOROMETHYL)QUINAZOLIN-4-AMINE. DR DrugBank; DB08247; 6-(CYCLOHEXYLMETHOXY)-8-ISOPROPYL-9H-PURIN-2-AMINE. DR DrugBank; DB08441; 6-BROMO-13-THIA-2,4,8,12,19-PENTAAZATRICYCLO[12.3.1.1~3,7~]NONADECA-1(18),3(19),4,6,14,16-HEXAENE 13,13-DIOXIDE. DR DrugBank; DB07203; 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE. DR DrugBank; DB08233; 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE. DR DrugBank; DB08312; 6-CYCLOHEXYLMETHYLOXY-5-NITROSO-PYRIMIDINE-2,4-DIAMINE. DR DrugBank; DB02407; 6-O-Cyclohexylmethyl Guanine. DR DrugBank; DB04006; [2-Amino-6-(2,6-Difluoro-Benzoyl)-Imidazo[1,2-a]Pyridin-3-Yl]-Phenyl-Methanone. DR DrugBank; DB02833; [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine. DR DrugBank; DB03496; Alvocidib. DR DrugBank; DB08142; AT-7519. DR DrugBank; DB06616; Bosutinib. DR DrugBank; DB07731; CAN-508. DR DrugBank; DB08218; HYDROXY(OXO)(3-{[(2Z)-4-[3-(1H-1,2,4-TRIAZOL-1-YLMETHYL)PHENYL]PYRIMIDIN-2(5H)-YLIDENE]AMINO}PHENYL)AMMONIUM. DR DrugBank; DB02950; Hymenialdisine. DR DrugBank; DB02052; Indirubin-3'-monoxime. DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid. DR DrugBank; DB04186; N'-(Pyrrolidino[2,1-B]Isoindolin-4-On-8-Yl)-N-(Pyridin-2-Yl)Urea. DR DrugBank; DB04101; N'-[4-(2,4-Dimethyl-1,3-thiazol-5-yl)-2-pyrimidinyl]-N-hydroxyimidoformamide. DR DrugBank; DB08768; N(6)-dimethylallyladenine. DR DrugBank; DB08538; N-((2-aminopyrimidin-5-yl)methyl)-5-(2,6-difluorophenyl)-3-ethylpyrazolo[1,5-a]pyrimidin-7-amine. DR DrugBank; DB07790; N-(2-METHOXYETHYL)-4-({4-[2-METHYL-1-(1-METHYLETHYL)-1H-IMIDAZOL-5-YL]PYRIMIDIN-2-YL}AMINO)BENZENESULFONAMIDE. DR DrugBank; DB06944; N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide. DR DrugBank; DB08133; N-(4-sulfamoylphenyl)-1H-indazole-3-carboxamide. DR DrugBank; DB07936; N-(4-{[(3S)-3-(dimethylamino)pyrrolidin-1-yl]carbonyl}phenyl)-5-fluoro-4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-amine. DR DrugBank; DB02647; N-(5-Cyclopropyl-1h-Pyrazol-3-Yl)Benzamide. DR DrugBank; DB08677; N-(5-Isopropyl-thiazol-2-YL)-2-pyridin-3-YL-acetamide. DR DrugBank; DB08066; N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE. DR DrugBank; DB07562; N-[4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-DIMETHYL-BENZENE-1,4-DIAMINE. DR DrugBank; DB02538; N-[4-(2-Methylimidazo[1,2-a]Pyridin-3-Yl)-2-Pyrimidinyl]Acetamide. DR DrugBank; DB07220; N-[5-(1,1-DIOXIDOISOTHIAZOLIDIN-2-YL)-1H-INDAZOL-3-YL]-2-(4-PIPERIDIN-1-YLPHENYL)ACETAMIDE. DR DrugBank; DB07164; N-cyclopropyl-4-pyrazolo[1,5-b]pyridazin-3-ylpyrimidin-2-amine. DR DrugBank; DB08122; N-Methyl-4-{[(2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]amino}benzenesulfonamide. DR DrugBank; DB08123; N-methyl-{4-[2-(7-oxo-6,7-dihydro-8H-[1,3]thiazolo[5,4-e]indol-8-ylidene)hydrazino]phenyl}methanesulfonamide. DR DrugBank; DB08135; N-phenyl-1H-pyrazole-3-carboxamide. DR DrugBank; DB07126; O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE. DR DrugBank; DB02116; Olomoucine. DR DrugBank; DB04662; OLOMOUCINE II. DR DrugBank; DB04607; PHENYLAMINOIMIDAZO(1,2-ALPHA)PYRIDINE. DR DrugBank; DB02733; Purvalanol. DR DrugBank; DB08094; RO-4584820. DR DrugBank; DB06195; Seliciclib. DR DrugBank; DB02010; Staurosporine. DR DrugBank; DB03428; SU9516. DR DrugBank; DB04669; TRIAZOLOPYRIMIDINE. DR DrugBank; DB15442; Trilaciclib. DR DrugBank; DB08694; Variolin B. DR DrugBank; DB08138; {[(2,6-difluorophenyl)carbonyl]amino}-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamide. DR DrugCentral; P24941; -. DR GuidetoPHARMACOLOGY; 1973; -. DR GlyGen; P24941; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P24941; -. DR PhosphoSitePlus; P24941; -. DR SwissPalm; P24941; -. DR BioMuta; CDK2; -. DR DMDM; 116051; -. DR CPTAC; CPTAC-3191; -. DR CPTAC; CPTAC-3192; -. DR CPTAC; CPTAC-3193; -. DR CPTAC; CPTAC-3194; -. DR EPD; P24941; -. DR jPOST; P24941; -. DR MassIVE; P24941; -. DR MaxQB; P24941; -. DR PaxDb; 9606-ENSP00000266970; -. DR PeptideAtlas; P24941; -. DR ProteomicsDB; 54241; -. [P24941-1] DR ProteomicsDB; 54242; -. [P24941-2] DR Pumba; P24941; -. DR Antibodypedia; 3404; 1989 antibodies from 50 providers. DR DNASU; 1017; -. DR Ensembl; ENST00000266970.9; ENSP00000266970.4; ENSG00000123374.11. [P24941-1] DR Ensembl; ENST00000354056.4; ENSP00000243067.4; ENSG00000123374.11. [P24941-2] DR GeneID; 1017; -. DR KEGG; hsa:1017; -. DR MANE-Select; ENST00000266970.9; ENSP00000266970.4; NM_001798.5; NP_001789.2. DR UCSC; uc001sit.5; human. [P24941-1] DR AGR; HGNC:1771; -. DR CTD; 1017; -. DR DisGeNET; 1017; -. DR GeneCards; CDK2; -. DR HGNC; HGNC:1771; CDK2. DR HPA; ENSG00000123374; Low tissue specificity. DR MIM; 116953; gene. DR neXtProt; NX_P24941; -. DR OpenTargets; ENSG00000123374; -. DR PharmGKB; PA101; -. DR VEuPathDB; HostDB:ENSG00000123374; -. DR eggNOG; KOG0594; Eukaryota. DR GeneTree; ENSGT00940000159517; -. DR HOGENOM; CLU_000288_181_1_1; -. DR InParanoid; P24941; -. DR OMA; HKEKCIY; -. DR OrthoDB; 244018at2759; -. DR PhylomeDB; P24941; -. DR TreeFam; TF101021; -. DR BRENDA; 2.7.11.22; 2681. DR PathwayCommons; P24941; -. DR Reactome; R-HSA-1538133; G0 and Early G1. DR Reactome; R-HSA-171319; Telomere Extension By Telomerase. DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress. DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase. DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends. DR Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation. DR Reactome; R-HSA-68911; G2 Phase. DR Reactome; R-HSA-68949; Orc1 removal from chromatin. DR Reactome; R-HSA-68962; Activation of the pre-replicative complex. DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-HSA-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes. DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition. DR Reactome; R-HSA-69231; Cyclin D associated events in G1. DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition. DR Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response. DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry. DR Reactome; R-HSA-8849470; PTK6 Regulates Cell Cycle. DR Reactome; R-HSA-912446; Meiotic recombination. DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. DR Reactome; R-HSA-9661069; Defective binding of RB1 mutants to E2F1,(E2F2, E2F3). DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P24941; -. DR SIGNOR; P24941; -. DR BioGRID-ORCS; 1017; 558 hits in 1210 CRISPR screens. DR ChiTaRS; CDK2; human. DR EvolutionaryTrace; P24941; -. DR GeneWiki; Cyclin-dependent_kinase_2; -. DR GenomeRNAi; 1017; -. DR Pharos; P24941; Tchem. DR PRO; PR:P24941; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P24941; Protein. DR Bgee; ENSG00000123374; Expressed in ventricular zone and 171 other cell types or tissues. DR ExpressionAtlas; P24941; baseline and differential. DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl. DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl. DR GO; GO:0097123; C:cyclin A1-CDK2 complex; IEA:Ensembl. DR GO; GO:0097124; C:cyclin A2-CDK2 complex; IDA:UniProtKB. DR GO; GO:0097134; C:cyclin E1-CDK2 complex; IEA:Ensembl. DR GO; GO:0097135; C:cyclin E2-CDK2 complex; IEA:Ensembl. DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:CAFA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl. DR GO; GO:0000805; C:X chromosome; IEA:Ensembl. DR GO; GO:0000806; C:Y chromosome; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030332; F:cyclin binding; IDA:UniProtKB. DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:UniProtKB. DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071732; P:cellular response to nitric oxide; TAS:UniProtKB. DR GO; GO:0090398; P:cellular senescence; TAS:Reactome. DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB. DR GO; GO:0051298; P:centrosome duplication; TAS:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IEA:GOC. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; TAS:UniProtKB. DR GO; GO:0006351; P:DNA-templated transcription; IEA:Ensembl. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:UniProtKB. DR GO; GO:0051321; P:meiotic cell cycle; TAS:UniProtKB. DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; TAS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0045740; P:positive regulation of DNA replication; TAS:Reactome. DR GO; GO:0032298; P:positive regulation of DNA-templated DNA replication initiation; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0031453; P:positive regulation of heterochromatin formation; IDA:UniProtKB. DR GO; GO:0043687; P:post-translational protein modification; IDA:CAFA. DR GO; GO:0006813; P:potassium ion transport; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL. DR GO; GO:1905784; P:regulation of anaphase-promoting complex-dependent catabolic process; TAS:Reactome. DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0007346; P:regulation of mitotic cell cycle; TAS:Reactome. DR GO; GO:0010033; P:response to organic substance; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd07860; STKc_CDK2_3; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR IDEAL; IID00034; -. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF521; CYCLIN-DEPENDENT KINASE 2; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P24941; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle; KW Cell division; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Endosome; KW Kinase; Magnesium; Meiosis; Metal-binding; Mitosis; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; S-nitrosylation; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..298 FT /note="Cyclin-dependent kinase 2" FT /id="PRO_0000085769" FT DOMAIN 4..286 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 127 FT /note="Proton acceptor" FT BINDING 10..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702" FT BINDING 33 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702" FT BINDING 81..83 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702" FT BINDING 86 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702" FT BINDING 129..132 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702" FT BINDING 132 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:21565702" FT BINDING 145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702" FT BINDING 145 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:21565702" FT SITE 9 FT /note="CDK7 binding" FT SITE 88..89 FT /note="CDK7 binding" FT SITE 166 FT /note="CDK7 binding" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 6 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 14 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:1396589, FT ECO:0000269|PubMed:17095507" FT MOD_RES 15 FT /note="Phosphotyrosine; by WEE1" FT /evidence="ECO:0000269|PubMed:1396589, FT ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332" FT MOD_RES 19 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 160 FT /note="Phosphothreonine; by CAK and CCRK" FT /evidence="ECO:0000269|PubMed:1396589, FT ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, FT ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, FT ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, FT ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995" FT VAR_SEQ 163..196 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_041998" FT VARIANT 15 FT /note="Y -> S (in dbSNP:rs3087335)" FT /id="VAR_016157" FT VARIANT 18 FT /note="V -> L (in dbSNP:rs11554376)" FT /id="VAR_053927" FT VARIANT 45 FT /note="P -> L (in a glioblastoma multiforme sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041972" FT VARIANT 290 FT /note="T -> S (in dbSNP:rs2069413)" FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.6" FT /id="VAR_019988" FT MUTAGEN 9 FT /note="K->F: Reduced phosphorylation by CAK." FT /evidence="ECO:0000269|PubMed:17373709" FT MUTAGEN 14 FT /note="T->A: 2-fold increase in activity." FT /evidence="ECO:0000269|PubMed:1396589" FT MUTAGEN 15 FT /note="Y->F: 2-fold increase in activity." FT /evidence="ECO:0000269|PubMed:1396589" FT MUTAGEN 88..89 FT /note="KK->EV: Reduced phosphorylation by CAK." FT /evidence="ECO:0000269|PubMed:17373709" FT MUTAGEN 160 FT /note="T->A: Abolishes activity." FT /evidence="ECO:0000269|PubMed:1396589" FT MUTAGEN 166 FT /note="L->R: Reduced phosphorylation by CAK and reduced FT kinase activity." FT /evidence="ECO:0000269|PubMed:17373709" FT CONFLICT 8..12 FT /note="EKIGE -> AQIGQ (in Ref. 5; BAA32794)" FT /evidence="ECO:0000305" FT CONFLICT 25..29 FT /note="LTGEV -> STGQM (in Ref. 5; BAA32794)" FT /evidence="ECO:0000305" FT CONFLICT 272..277 FT /note="NKRISA -> YKRFST (in Ref. 5; BAA32794)" FT /evidence="ECO:0000305" FT CONFLICT 286..287 FT /note="FQ -> LE (in Ref. 5; BAA32794)" FT /evidence="ECO:0000305" FT STRAND 3..12 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 14..23 FT /evidence="ECO:0007829|PDB:6Q4G" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 29..34 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:4GCJ" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:2CCH" FT HELIX 46..54 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 66..72 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 75..81 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 87..93 FT /evidence="ECO:0007829|PDB:6Q4G" FT TURN 94..97 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 101..120 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:6Q48" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 148..152 FT /evidence="ECO:0007829|PDB:6Q4G" FT TURN 153..156 FT /evidence="ECO:0007829|PDB:6Q4D" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:3RAI" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:7UXI" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 171..174 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:1OKW" FT HELIX 183..198 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 208..219 FT /evidence="ECO:0007829|PDB:6Q4G" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:6Q4G" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:1GY3" FT HELIX 257..266 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 271..273 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 277..281 FT /evidence="ECO:0007829|PDB:6Q4G" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:6Q4G" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:1W98" SQ SEQUENCE 298 AA; 33930 MW; F90A0F4E70910B51 CRC64; MENFQKVEKI GEGTYGVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR EISLLKELNH PNIVKLLDVI HTENKLYLVF EFLHQDLKKF MDASALTGIP LPLIKSYLFQ LLQGLAFCHS HRVLHRDLKP QNLLINTEGA IKLADFGLAR AFGVPVRTYT HEVVTLWYRA PEILLGCKYY STAVDIWSLG CIFAEMVTRR ALFPGDSEID QLFRIFRTLG TPDEVVWPGV TSMPDYKPSF PKWARQDFSK VVPPLDEDGR SLLSQMLHYD PNKRISAKAA LAHPFFQDVT KPVPHLRL //