CDK2_HUMAN
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 03-AUG-2022, entry version 258.
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=4; 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=25; 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/";
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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; 7NVQ; X-ray; 2.05 A; A=1-298.
DR PDB; 7RA5; X-ray; 1.67 A; A=1-298.
DR PDB; 7VDU; X-ray; 1.53 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; 7NVQ; -.
DR PDBsum; 7RA5; -.
DR PDBsum; 7VDU; -.
DR AlphaFoldDB; P24941; -.
DR SMR; P24941; -.
DR BioGRID; 107452; 766.
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; 183.
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 EPD; P24941; -.
DR jPOST; P24941; -.
DR MassIVE; P24941; -.
DR MaxQB; P24941; -.
DR PaxDb; P24941; -.
DR PeptideAtlas; P24941; -.
DR PRIDE; P24941; -.
DR ProteomicsDB; 54241; -. [P24941-1]
DR ProteomicsDB; 54242; -. [P24941-2]
DR Antibodypedia; 3404; 1749 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 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 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; 535 hits in 1128 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 169 other tissues.
DR ExpressionAtlas; P24941; baseline and differential.
DR Genevisible; P24941; HS.
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: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; IGI:ARUK-UCL.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; TAS:UniProtKB.
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:0016572; P:histone phosphorylation; IDA:CAFA.
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:0032298; P:positive regulation of DNA-templated DNA replication initiation; IEA:Ensembl.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
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:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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 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
