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Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2) (p33 protein kinase)

 CDK2_HUMAN              Reviewed;         298 AA.
P24941; A8K7C6; O75100;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 2.
22-NOV-2017, entry version 225.
RecName: Full=Cyclin-dependent kinase 2;
EC=2.7.11.22;
AltName: Full=Cell division protein kinase 2;
AltName: Full=p33 protein kinase;
Name=CDK2; Synonyms=CDKN2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1714386;
Elledge S.J., Spottswood M.R.;
"A new human p34 protein kinase, CDK2, identified by complementation
of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of
Xenopus Eg1.";
EMBO J. 10:2653-2659(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1653904; DOI=10.1038/353174a0;
Tsai L.-H., Harlow E., Meyerson M.;
"Isolation of the human cdk2 gene that encodes the cyclin A- and
adenovirus E1A-associated p33 kinase.";
Nature 353:174-177(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1717994; DOI=10.1073/pnas.88.20.9006;
Ninomiya-Tsuji J., Nomoto S., Yasuda H., Reed S.I., Matsumoto K.;
"Cloning of a human cDNA encoding a CDC2-related kinase by
complementation of a budding yeast cdc28 mutation.";
Proc. Natl. Acad. Sci. U.S.A. 88:9006-9010(1991).
[4]
NUCLEOTIDE SEQUENCE (ISOFORM 2).
Nishikawa T., Ohta T., Fukuda M., Ogata H., Okamoto K., Isohashi F.,
Arima K., Yamaguchi S.;
"Sequence of deletion type cdk2 variant in human breast cancer.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-290.
NIEHS SNPs program;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160, AND MUTAGENESIS OF
THR-14; TYR-15 AND THR-160.
PubMed=1396589;
Gu Y., Rosenblatt J., O'Morgan D.O.;
"Cell cycle regulation of CDK2 activity by phosphorylation of Thr160
and Tyr15.";
EMBO J. 11:3995-4005(1992).
[12]
ENZYME REGULATION BY ROSCOVITINE AND OLOMOUCINE.
PubMed=9030781; DOI=10.1111/j.1432-1033.1997.t01-2-00527.x;
Meijer L., Borgne A., Mulner O., Chong J.P.J., Blow J.J., Inagaki N.,
Inagaki M., Delcros J.-G., Moulinoux J.-P.;
"Biochemical and cellular effects of roscovitine, a potent and
selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and
cdk5.";
Eur. J. Biochem. 243:527-536(1997).
[13]
FUNCTION AS RB1 KINASE, AND INTERACTION WITH CYCLIN E.
PubMed=10499802; DOI=10.1016/S0092-8674(00)81519-6;
Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C.;
"Cdk phosphorylation triggers sequential intramolecular interactions
that progressively block Rb functions as cells move through G1.";
Cell 98:859-869(1999).
[14]
FUNCTION AS NPM1 KINASE.
PubMed=11051553; DOI=10.1016/S0092-8674(00)00093-3;
Okuda M., Horn H.F., Tarapore P., Tokuyama Y., Smulian A.G.,
Chan P.K., Knudsen E.S., Hofmann I.A., Snyder J.D., Bove K.E.,
Fukasawa K.;
"Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome
duplication.";
Cell 103:127-140(2000).
[15]
FUNCTION AS NPAT KINASE.
PubMed=10995386; DOI=10.1101/gad.827700;
Zhao J., Kennedy B.K., Lawrence B.D., Barbie D.A., Matera A.G.,
Fletcher J.A., Harlow E.;
"NPAT links cyclin E-Cdk2 to the regulation of replication-dependent
histone gene transcription.";
Genes Dev. 14:2283-2297(2000).
[16]
FUNCTION AS NPAT KINASE, AND SUBCELLULAR LOCATION.
PubMed=10995387; DOI=10.1101/gad.829500;
Ma T., Van Tine B.A., Wei Y., Garrett M.D., Nelson D., Adams P.D.,
Wang J., Qin J., Chow L.T., Harper J.W.;
"Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2
in Cajal bodies promotes histone gene transcription.";
Genes Dev. 14:2298-2313(2000).
[17]
FUNCTION AS P53/TP53 KINASE, AND INTERACTION WITH CYCLIN A AND CYCLIN
B1.
PubMed=10884347; DOI=10.1006/jmbi.2000.3830;
Luciani M.G., Hutchins J.R.A., Zheleva D., Hupp T.R.;
"The C-terminal regulatory domain of p53 contains a functional docking
site for cyclin A.";
J. Mol. Biol. 300:503-518(2000).
[18]
FUNCTION AS CDK7 KINASE, AND PHOSPHORYLATION BY CDK7.
PubMed=11113184; DOI=10.1128/MCB.21.1.88-99.2001;
Garrett S., Barton W.A., Knights R., Jin P., Morgan D.O., Fisher R.P.;
"Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed
by substrate specificity determinants outside the T loop.";
Mol. Cell. Biol. 21:88-99(2001).
[19]
INTERACTION WITH CCNB3.
PubMed=12185076; DOI=10.1074/jbc.M203951200;
Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S.,
Wang X.-Y., Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.;
"Characterization and expression of mammalian cyclin b3, a
prepachytene meiotic cyclin.";
J. Biol. Chem. 277:41960-41969(2002).
[20]
INTERACTION WITH SPDYA.
PubMed=11980914; DOI=10.1083/jcb.200109045;
Porter L.A., Dellinger R.W., Tynan J.A., Barnes E.A., Kong M.,
Lenormand J.-L., Donoghue D.J.;
"Human Speedy: a novel cell cycle regulator that enhances
proliferation through activation of Cdk2.";
J. Cell Biol. 157:357-366(2002).
[21]
INTERACTION WITH SPDYA.
PubMed=12839962;
Barnes E.A., Porter L.A., Lenormand J.-L., Dellinger R.W.,
Donoghue D.J.;
"Human Spy1 promotes survival of mammalian cells following DNA
damage.";
Cancer Res. 63:3701-3707(2003).
[22]
FUNCTION.
PubMed=12944431; DOI=10.1242/dev.00731;
Terret M.E., Lefebvre C., Djiane A., Rassinier P., Moreau J., Maro B.,
Verlhac M.H.;
"DOC1R: a MAP kinase substrate that control microtubule organization
of metaphase II mouse oocytes.";
Development 130:5169-5177(2003).
[23]
INTERACTION WITH SPDYA, AND IDENTIFICATION IN A COMPLEX WITH CDKN1B
AND SPDYA.
PubMed=12972555; DOI=10.1091/mbc.E02-12-0820;
Porter L.A., Kong-Beltran M., Donoghue D.J.;
"Spy1 interacts with p27Kip1 to allow G1/S progression.";
Mol. Biol. Cell 14:3664-3674(2003).
[24]
INTERACTION WITH UHRF2, AND IDENTIFICATION IN A COMPLEX WITH UHRF2 AND
CCNE1.
PubMed=15178429; DOI=10.1016/j.bbrc.2004.04.190;
Li Y., Mori T., Hata H., Homma Y., Kochi H.;
"NIRF induces G1 arrest and associates with Cdk2.";
Biochem. Biophys. Res. Commun. 319:464-468(2004).
[25]
INTERACTION WITH CEBPA.
PubMed=15107404; DOI=10.1101/gad.1183304;
Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
"Liver tumors escape negative control of proliferation via PI3K/Akt-
mediated block of C/EBP alpha growth inhibitory activity.";
Genes Dev. 18:912-925(2004).
[26]
PHOSPHORYLATION AT THR-160.
PubMed=14597612; DOI=10.1074/jbc.M309995200;
Liu Y., Wu C., Galaktionov K.;
"p42, a novel cyclin-dependent kinase-activating kinase in mammalian
cells.";
J. Biol. Chem. 279:4507-4514(2004).
[27]
INTERACTION WITH SPDYA AND SPDYC.
PubMed=15611625; DOI=10.4161/cc.4.1.1347;
Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.;
"Identification and comparative analysis of multiple mammalian
Speedy/Ringo proteins.";
Cell Cycle 4:155-165(2005).
[28]
FUNCTION AS BRCA2 KINASE.
PubMed=15800615; DOI=10.1038/nature03404;
Esashi F., Christ N., Gannon J., Liu Y., Hunt T., Jasin M., West S.C.;
"CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for
recombinational repair.";
Nature 434:598-604(2005).
[29]
PHOSPHORYLATION BY CAK, MUTAGENESIS OF LYS-9; 88-LYS-LYS-89 AND
LEU-166, AND INTERACTION WITH CDK7.
PubMed=17373709; DOI=10.1002/prot.21370;
Lolli G., Johnson L.N.;
"Recognition of Cdk2 by Cdk7.";
Proteins 67:1048-1059(2007).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[31]
FUNCTION IN MITOSE REGULATION, AND SUBCELLULAR LOCATION.
PubMed=18372919; DOI=10.1038/onc.2008.74;
De Boer L., Oakes V., Beamish H., Giles N., Stevens F.,
Somodevilla-Torres M., Desouza C., Gabrielli B.;
"Cyclin A/cdk2 coordinates centrosomal and nuclear mitotic events.";
Oncogene 27:4261-4268(2008).
[32]
INTERACTION WITH CACUL1.
PubMed=19829063; DOI=10.4161/cc.8.21.9955;
Kong Y., Nan K., Yin Y.;
"Identification and characterization of CAC1 as a novel CDK2-
associated cullin.";
Cell Cycle 8:3552-3561(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[36]
FUNCTION IN VITAMIN D-MEDIATED GROWTH INHIBITION, SUBCELLULAR
LOCATION, ENZYME REGULATION, AND PHOSPHORYLATION AT THR-160.
PubMed=20147522; DOI=10.1210/en.2009-1116;
Flores O., Wang Z., Knudsen K.E., Burnstein K.L.;
"Nuclear targeting of cyclin-dependent kinase 2 reveals essential
roles of cyclin-dependent kinase 2 localization and cyclin E in
vitamin D-mediated growth inhibition.";
Endocrinology 151:896-908(2010).
[37]
FUNCTION, AND S-NITROSYLATION.
PubMed=20079829; DOI=10.1016/j.freeradbiomed.2010.01.004;
Kumar S., Barthwal M.K., Dikshit M.;
"Cdk2 nitrosylation and loss of mitochondrial potential mediate NO-
dependent biphasic effect on HL-60 cell cycle.";
Free Radic. Biol. Med. 48:851-861(2010).
[38]
PHOSPHORYLATION AT THR-160 BY CAK, AND DEPHOSPHORYLATION BY CDC25A.
PubMed=20360007; DOI=10.1074/jbc.M109.096552;
Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.;
"Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B
at the G2/M transition.";
J. Biol. Chem. 285:16978-16990(2010).
[39]
FUNCTION AS EZH2 KINASE.
PubMed=20935635; DOI=10.1038/ncb2116;
Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A.,
Simon J.A., Huang H.;
"Cyclin-dependent kinases regulate epigenetic gene silencing through
phosphorylation of EZH2.";
Nat. Cell Biol. 12:1108-1114(2010).
[40]
FUNCTION IN DNA DAMAGE CHECKPOINT.
PubMed=20195506; DOI=10.1371/journal.pgen.1000863;
Chung J.H., Bunz F.;
"Cdk2 is required for p53-independent G2/M checkpoint control.";
PLoS Genet. 6:E1000863-E1000863(2010).
[41]
FUNCTION AS MYC KINASE.
PubMed=19966300; DOI=10.1073/pnas.0900121106;
Hydbring P., Bahram F., Su Y., Tronnersjoe S., Hoegstrand K.,
von der Lehr N., Sharifi H.R., Lilischkis R., Hein N., Wu S.,
Vervoorts J., Henriksson M., Grandien A., Luescher B., Larsson L.-G.;
"Phosphorylation by Cdk2 is required for Myc to repress Ras-induced
senescence in cotransformation.";
Proc. Natl. Acad. Sci. U.S.A. 107:58-63(2010).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[43]
INTERACTION WITH CEP63.
PubMed=21406398; DOI=10.1158/0008-5472.CAN-10-2684;
Loffler H., Fechter A., Matuszewska M., Saffrich R., Mistrik M.,
Marhold J., Hornung C., Westermann F., Bartek J., Kramer A.;
"Cep63 recruits Cdk1 to the centrosome: implications for regulation of
mitotic entry, centrosome amplification, and genome maintenance.";
Cancer Res. 71:2129-2139(2011).
[44]
FUNCTION AS CTNNB1 KINASE, SUBCELLULAR LOCATION, AND INTERACTION WITH
PTPN6 AND CTNNB1.
PubMed=21262353; DOI=10.1016/j.cellsig.2011.01.019;
Fiset A., Xu E., Bergeron S., Marette A., Pelletier G.,
Siminovitch K.A., Olivier M., Beauchemin N., Faure R.L.;
"Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and
regulates insulin internalization.";
Cell. Signal. 23:911-919(2011).
[45]
INHIBITORS.
PubMed=21684737; DOI=10.1016/j.bmcl.2011.05.081;
Lee J., Kim K.H., Jeong S.;
"Discovery of a novel class of 2-aminopyrimidines as CDK1 and CDK2
inhibitors.";
Bioorg. Med. Chem. Lett. 21:4203-4205(2011).
[46]
FUNCTION AS USP37 KINASE.
PubMed=21596315; DOI=10.1016/j.molcel.2011.03.027;
Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G.,
Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.;
"Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and
promote S phase entry.";
Mol. Cell 42:511-523(2011).
[47]
FUNCTION IN CELL CYCLE REGULATION.
PubMed=21319273; DOI=10.1002/stem.620;
Neganova I., Vilella F., Atkinson S.P., Lloret M., Passos J.F.,
von Zglinicki T., O'Connor J.-E., Burks D., Jones R., Armstrong L.,
Lako M.;
"An important role for CDK2 in G1 to S checkpoint activation and DNA
damage response in human embryonic stem cells.";
Stem Cells 29:651-659(2011).
[48]
REVIEW ON DNA REPAIR, AND INTERACTION WITH CDKN1A/P21.
PubMed=19445729; DOI=10.1186/1747-1028-4-9;
Satyanarayana A., Kaldis P.;
"A dual role of Cdk2 in DNA damage response.";
Cell Div. 4:9-9(2009).
[49]
REVIEW ON CELL CYCLE CONTROL, INHIBITORS, AND GENE FAMILY.
PubMed=19238148; DOI=10.1038/nrc2602;
Malumbres M., Barbacid M.;
"Cell cycle, CDKs and cancer: a changing paradigm.";
Nat. Rev. Cancer 9:153-166(2009).
[50]
REVIEW, AND GENE FAMILY.
PubMed=19561645; DOI=10.1038/onc.2009.170;
Satyanarayana A., Kaldis P.;
"Mammalian cell-cycle regulation: several Cdks, numerous cyclins and
diverse compensatory mechanisms.";
Oncogene 28:2925-2939(2009).
[51]
REVIEW ON SENESCENCE.
PubMed=20713526; DOI=10.1158/0008-5472.CAN-10-1383;
Hydbring P., Larsson L.-G.;
"Tipping the balance: Cdk2 enables Myc to suppress senescence.";
Cancer Res. 70:6687-6691(2010).
[52]
REVIEW ON INHIBITORS.
PubMed=21517772; DOI=10.2174/092986711795590110;
Wang Q., Su L., Liu N., Zhang L., Xu W., Fang H.;
"Cyclin dependent kinase 1 inhibitors: a review of recent progress.";
Curr. Med. Chem. 18:2025-2043(2011).
[53]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[54]
INTERACTION WITH CYCLIN E; CYCLIN A AND CDK2AP2, AND PHOSPHORYLATION.
PubMed=23781148; DOI=10.7150/ijbs.5763;
Liu Q., Liu X., Gao J., Shi X., Hu X., Wang S., Luo Y.;
"Overexpression of DOC-1R inhibits cell cycle G1/S transition by
repressing CDK2 expression and activation.";
Int. J. Biol. Sci. 9:541-549(2013).
[55]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=8510751; DOI=10.1038/363595a0;
de Bondt H.L., Rosenblatt J., Jancarik J., Jones H.D., Morgan D.O.,
Kim S.-H.;
"Crystal structure of cyclin-dependent kinase 2.";
Nature 363:595-602(1993).
[56]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CYCLIN A.
PubMed=7630397; DOI=10.1038/376313a0;
Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J.,
Massague J., Pavletich N.P.;
"Mechanism of CDK activation revealed by the structure of a cyclinA-
CDK2 complex.";
Nature 376:313-320(1995).
[57]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITG CKS1.
PubMed=8601310; DOI=10.1016/S0092-8674(00)81065-X;
Bourne Y., Watson M.H., Hickey M.J., Holmes W., Rocque W., Reed S.I.,
Tainer J.A.;
"Crystal structure and mutational analysis of the human CDK2 kinase
complex with cell cycle-regulatory protein CksHs1.";
Cell 84:863-874(1996).
[58]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=8917641; DOI=10.1021/jm960402a;
Schulze-Gahmen U., de Bondt H.L., Kim S.-H.;
"High-resolution crystal structures of human cyclin-dependent kinase 2
with and without ATP: bound waters and natural ligand as guides for
inhibitor design.";
J. Med. Chem. 39:4540-4546(1996).
[59]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CCNA2 AND
CDKN1B.
PubMed=8684460; DOI=10.1038/382325a0;
Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.;
"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor
bound to the cyclin A-Cdk2 complex.";
Nature 382:325-331(1996).
[60]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CG2A.
PubMed=8756328; DOI=10.1038/nsb0896-696;
Russo A.A., Jeffrey P.D., Pavletich N.P.;
"Structural basis of cyclin-dependent kinase activation by
phosphorylation.";
Nat. Struct. Biol. 3:696-700(1996).
[61]
X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH L868276.
PubMed=8610110; DOI=10.1073/pnas.93.7.2735;
de Azevedo W.F. Jr., Mueller-Dieckmann H.-J., Schulze-Gahmen U.,
Worland P.J., Sausville E., Kim S.-H.;
"Structural basis for specificity and potency of a flavonoid inhibitor
of human CDK2, a cell cycle kinase.";
Proc. Natl. Acad. Sci. U.S.A. 93:2735-2740(1996).
[62]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH STAUROSPORINE,
AND ENZYME REGULATION.
PubMed=9334743; DOI=10.1038/nsb1097-796;
Lawrie A.M., Noble M.E.M., Tunnah P., Brown N.R., Johnson L.N.,
Endicott J.A.;
"Protein kinase inhibition by staurosporine revealed in details of the
molecular interaction with CDK2.";
Nat. Struct. Biol. 4:796-801(1997).
[63]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
PubMed=9677190; DOI=10.1126/science.281.5376.533;
Gray N.S., Wodicka L., Thunnissen A.-M.W.H., Norman T.C., Kwon S.,
Espinoza F.H., Morgan D.O., Barnes G., Leclerc S., Meijer L.,
Kim S.H., Lockhart D.J., Schultz P.G.;
"Exploiting chemical libraries, structure, and genomics in the search
for kinase inhibitors.";
Science 281:533-538(1998).
[64]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
PHOSPHORYLATION AT THR-160.
PubMed=16325401; DOI=10.1016/j.bmcl.2005.11.048;
Richardson C.M., Williamson D.S., Parratt M.J., Borgognoni J.,
Cansfield A.D., Dokurno P., Francis G.L., Howes R., Moore J.D.,
Murray J.B., Robertson A., Surgenor A.E., Torrance C.J.;
"Triazolo[1,5-a]pyrimidines as novel CDK2 inhibitors: protein
structure-guided design and SAR.";
Bioorg. Med. Chem. Lett. 16:1353-1357(2006).
[65]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
PHOSPHORYLATION AT THR-160.
PubMed=17570665; DOI=10.1016/j.bmcl.2007.04.110;
Richardson C.M., Nunns C.L., Williamson D.S., Parratt M.J.,
Dokurno P., Howes R., Borgognoni J., Drysdale M.J., Finch H.,
Hubbard R.E., Jackson P.S., Kierstan P., Lentzen G., Moore J.D.,
Murray J.B., Simmonite H., Surgenor A.E., Torrance C.J.;
"Discovery of a potent CDK2 inhibitor with a novel binding mode, using
virtual screening and initial, structure-guided lead scoping.";
Bioorg. Med. Chem. Lett. 17:3880-3885(2007).
[66]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-288 IN COMPLEX WITH CCNB1,
AND FUNCTION.
PubMed=17495531; DOI=10.4161/cc.6.11.4278;
Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R.,
Johnson L.N.;
"Cyclin B and cyclin A confer different substrate recognition
properties on CDK2.";
Cell Cycle 6:1350-1359(2007).
[67]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ATP, AND
PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160.
PubMed=17095507; DOI=10.1074/jbc.M609151200;
Welburn J.P.I., Tucker J.A., Johnson T., Lindert L., Morgan M.,
Willis A., Noble M.E.M., Endicott J.A.;
"How tyrosine 15 phosphorylation inhibits the activity of cyclin-
dependent kinase 2-cyclin A.";
J. Biol. Chem. 282:3173-3181(2007).
[68]
X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=17937404; DOI=10.1002/bip.20868;
Fischmann T.O., Hruza A., Duca J.S., Ramanathan L., Mayhood T.,
Windsor W.T., Le H.V., Guzi T.J., Dwyer M.P., Paruch K., Doll R.J.,
Lees E., Parry D., Seghezzi W., Madison V.;
"Structure-guided discovery of cyclin-dependent kinase inhibitors.";
Biopolymers 89:372-379(2008).
[69]
X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
PubMed=18656911; DOI=10.1021/jm800382h;
Wyatt P.G., Woodhead A.J., Berdini V., Boulstridge J.A., Carr M.G.,
Cross D.M., Davis D.J., Devine L.A., Early T.R., Feltell R.E.,
Lewis E.J., McMenamin R.L., Navarro E.F., O'Brien M.A., O'Reilly M.,
Reule M., Saxty G., Seavers L.C., Smith D.M., Squires M.S.,
Trewartha G., Walker M.T., Woolford A.J.;
"Identification of N-(4-piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-
pyrazole-3-carboxamide (AT7519), a novel cyclin dependent kinase
inhibitor using fragment-based X-ray crystallography and structure
based drug design.";
J. Med. Chem. 51:4986-4999(2008).
[70]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-296 IN COMPLEX WITH ATP
AND MAGNESIUM, COFACTOR, AND PHOSPHORYLATION AT THR-160.
PubMed=21565702; DOI=10.1016/j.str.2011.02.016;
Bao Z.Q., Jacobsen D.M., Young M.A.;
"Briefly bound to activate: transient binding of a second catalytic
magnesium activates the structure and dynamics of CDK2 kinase for
catalysis.";
Structure 19:675-690(2011).
[71]
VARIANTS [LARGE SCALE ANALYSIS] LEU-45 AND SER-290.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[72]
INTERACTION WITH ANKRD17.
PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
Menning M., Kufer T.A.;
"A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
Nod2-mediated inflammatory responses.";
FEBS Lett. 587:2137-2142(2013).
-!- FUNCTION: Serine/threonine-protein kinase involved in the control
of the cell cycle; essential for meiosis, but dispensable for
mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1,
BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and
DNA. Acts at the G1-S transition to promote the E2F
transcriptional program and the initiation of DNA synthesis, and
modulates G2 progression; controls the timing of entry into
mitosis/meiosis by controlling the subsequent activation of cyclin
B/CDK1 by phosphorylation, and coordinates the activation of
cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role
in orchestrating a fine balance between cellular proliferation,
cell death, and DNA repair in human embryonic stem cells (hESCs).
Activity of CDK2 is maximal during S phase and G2; activated by
interaction with cyclin E during the early stages of DNA synthesis
to permit G1-S transition, and subsequently activated by cyclin A2
(cyclin A1 in germ cells) during the late stages of DNA
replication to drive the transition from S phase to mitosis, the
G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and
epigenetic gene silencing. Phosphorylates CABLES1 (By similarity).
Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced
senescence by phosphorylating MYC. Involved in G1-S phase DNA
damage checkpoint that prevents cells with damaged DNA from
initiating mitosis; regulates homologous recombination-dependent
repair by phosphorylating BRCA2, this phosphorylation is low in S
phase when recombination is active, but increases as cells
progress towards mitosis. In response to DNA damage, double-strand
break repair by homologous recombination a reduction of CDK2-
mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs
its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2
promotes its dissociates from unduplicated centrosomes, thus
initiating centrosome duplication. Cyclin E/CDK2-mediated
phosphorylation of NPAT at G1-S transition and until prophase
stimulates the NPAT-mediated activation of histone gene
transcription during S phase. Required for vitamin D-mediated
growth inhibition by being itself inactivated. Involved in the
nitric oxide- (NO) mediated signaling in a
nitrosylation/activation-dependent manner. USP37 is activated by
phosphorylation and thus triggers G1-S transition. CTNNB1
phosphorylation regulates insulin internalization. Phosphorylates
FOXP3 and negatively regulates its transcriptional activity and
protein stability (By similarity). Phosphorylates CDK2AP2
(PubMed:12944431). {ECO:0000250|UniProtKB:P97377,
ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:10884347,
ECO:0000269|PubMed:10995386, ECO:0000269|PubMed:10995387,
ECO:0000269|PubMed:11051553, ECO:0000269|PubMed:11113184,
ECO:0000269|PubMed:12944431, ECO:0000269|PubMed:15800615,
ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:18372919,
ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20079829,
ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20195506,
ECO:0000269|PubMed:20935635, ECO:0000269|PubMed:21262353,
ECO:0000269|PubMed:21319273, ECO:0000269|PubMed:21596315}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:21565702};
Note=Binds 2 Mg(2+) ions. {ECO:0000269|PubMed:21565702};
-!- ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
the enzyme, while phosphorylation at Thr-160 activates it.
Inhibited by 1,25-dihydroxyvitamin D(3) (1,25-(OH)(2)D(3)), AG-
024322, N-(4-Piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-
pyrazole-3-carboxamide (AT7519), R547 (Ro-4584820), purine,
pyrimidine and pyridine derivatives, 2-aminopyrimidines,
paullones, thiazo derivatives, macrocyclic quinoxalin-2-one,
pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine, 2-(1-
ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine
(roscovitine, seliciclib and CYC202), SNS-032 (BMS-387032),
triazolo[1,5-a]pyrimidines, staurosporine and olomoucine.
Stimulated by MYC. Inactivated by CDKN1A (p21).
{ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:9030781,
ECO:0000269|PubMed:9334743}.
-!- SUBUNIT: Found in a complex with CABLES1, CCNA1 and CCNE1.
Interacts with CABLES1 (By similarity). Interacts with UHRF2. Part
of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with
the Speedy/Ringo proteins SPDYA and SPDYC. Found in a complex with
both SPDYA and CDKN1B/KIP1. Binds to RB1 and CDK7. Binding to
CDKN1A (p21) leads to CDK2/cyclin E inactivation at the G1-S phase
DNA damage checkpoint, thereby arresting cells at the G1-S
transition during DNA repair. Associated with PTPN6 and beta-
catenin/CTNNB1. Interacts with CACUL1. May interact with CEP63.
Interacts with ANKRD17. Interacts with CEBPA (when phosphorylated)
(PubMed:15107404). Forms a ternary complex with CCNA2 and CDKN1B;
CDKN1B inhibits the kinase activity of CDK2 through conformational
rearrangements (PubMed:8684460). Interacts with cyclins A, B1, B3,
D, or E (PubMed:10499802, PubMed:10884347, PubMed:12185076,
PubMed:23781148). Interacts with CDK2AP2 (PubMed:23781148).
{ECO:0000250|UniProtKB:P97377, ECO:0000250|UniProtKB:Q63699,
ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:10884347,
ECO:0000269|PubMed:11980914, ECO:0000269|PubMed:12185076,
ECO:0000269|PubMed:12839962, ECO:0000269|PubMed:12972555,
ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:15178429,
ECO:0000269|PubMed:15611625, ECO:0000269|PubMed:16325401,
ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17373709,
ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:17570665,
ECO:0000269|PubMed:17937404, ECO:0000269|PubMed:18656911,
ECO:0000269|PubMed:19445729, ECO:0000269|PubMed:19829063,
ECO:0000269|PubMed:21262353, ECO:0000269|PubMed:21406398,
ECO:0000269|PubMed:21565702, ECO:0000269|PubMed:23711367,
ECO:0000269|PubMed:23781148, ECO:0000269|PubMed:7630397,
ECO:0000269|PubMed:8610110, ECO:0000269|PubMed:8684460,
ECO:0000269|PubMed:8756328, ECO:0000269|PubMed:9334743}.
-!- INTERACTION:
P20248:CCNA2; NbExp=25; IntAct=EBI-375096, EBI-457097;
P30274:CCNA2 (xeno); NbExp=2; IntAct=EBI-375096, EBI-15688654;
P51943:Ccna2 (xeno); NbExp=2; IntAct=EBI-375096, EBI-846980;
O95067:CCNB2; NbExp=3; IntAct=EBI-375096, EBI-375024;
P24385:CCND1; NbExp=3; IntAct=EBI-375096, EBI-375001;
P24864:CCNE1; NbExp=18; IntAct=EBI-375096, EBI-519526;
O96020:CCNE2; NbExp=10; IntAct=EBI-375096, EBI-375033;
P51946:CCNH; NbExp=3; IntAct=EBI-375096, EBI-741406;
P50613:CDK7; NbExp=3; IntAct=EBI-375096, EBI-1245958;
P38936:CDKN1A; NbExp=25; IntAct=EBI-375096, EBI-375077;
P46527:CDKN1B; NbExp=23; IntAct=EBI-375096, EBI-519280;
Q16667:CDKN3; NbExp=7; IntAct=EBI-375096, EBI-1031527;
P61024:CKS1B; NbExp=6; IntAct=EBI-375096, EBI-456371;
P03129:E7 (xeno); NbExp=2; IntAct=EBI-375096, EBI-866453;
Q09472:EP300; NbExp=5; IntAct=EBI-375096, EBI-447295;
Q969H0-4:FBXW7; NbExp=2; IntAct=EBI-375096, EBI-6502391;
Q08619:Ifi205b (xeno); NbExp=2; IntAct=EBI-375096, EBI-8064290;
Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-375096, EBI-81279;
O95835:LATS1; NbExp=4; IntAct=EBI-375096, EBI-444209;
Q8TD08:MAPK15; NbExp=4; IntAct=EBI-375096, EBI-1383794;
P06400:RB1; NbExp=3; IntAct=EBI-375096, EBI-491274;
Q9UQR0:SCML2; NbExp=3; IntAct=EBI-375096, EBI-2513111;
Q9UQR0-1:SCML2; NbExp=7; IntAct=EBI-375096, EBI-16087037;
Q9UBI4:STOML1; NbExp=2; IntAct=EBI-375096, EBI-2681162;
Q96PU4:UHRF2; NbExp=5; IntAct=EBI-375096, EBI-625304;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. Nucleus, Cajal body. Cytoplasm.
Endosome. Note=Localized at the centrosomes in late G2 phase after
separation of the centrosomes but before the start of prophase.
Nuclear-cytoplasmic trafficking is mediated during the inhibition
by 1,25-(OH)(2)D(3).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P24941-1; Sequence=Displayed;
Name=2; Synonyms=CDK2deltaT;
IsoId=P24941-2; Sequence=VSP_041998;
-!- INDUCTION: Induced transiently by TGFB1 at an early phase of
TGFB1-mediated apoptosis.
-!- PTM: Phosphorylated at Thr-160 by CDK7 in a CAK complex.
Phosphorylation at Thr-160 promotes kinase activity, whereas
phosphorylation at Tyr-15 by WEE1 reduces slightly kinase
activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2
phases before being dephosphorylated by CDC25A.
{ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:1396589,
ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401,
ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17373709,
ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522,
ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702,
ECO:0000269|PubMed:23781148}.
-!- PTM: Nitrosylated after treatment with nitric oxide (DETA-NO).
{ECO:0000269|PubMed:20079829}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdk2/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X61622; CAA43807.1; -; mRNA.
EMBL; X62071; CAA43985.1; -; mRNA.
EMBL; M68520; AAA35667.1; -; mRNA.
EMBL; AB012305; BAA32794.1; -; mRNA.
EMBL; BT006821; AAP35467.1; -; mRNA.
EMBL; AF512553; AAM34794.1; -; Genomic_DNA.
EMBL; AK291941; BAF84630.1; -; mRNA.
EMBL; AC025162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC034102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96858.1; -; Genomic_DNA.
EMBL; BC003065; AAH03065.1; -; mRNA.
CCDS; CCDS8898.1; -. [P24941-1]
CCDS; CCDS8899.1; -. [P24941-2]
PIR; A41227; A41227.
RefSeq; NP_001277159.1; NM_001290230.1.
RefSeq; NP_001789.2; NM_001798.4. [P24941-1]
RefSeq; NP_439892.2; NM_052827.3. [P24941-2]
UniGene; Hs.19192; -.
UniGene; Hs.689624; -.
PDB; 1AQ1; X-ray; 2.00 A; A=1-298.
PDB; 1B38; X-ray; 2.00 A; A=1-298.
PDB; 1B39; X-ray; 2.10 A; A=1-298.
PDB; 1BUH; X-ray; 2.60 A; A=1-298.
PDB; 1CKP; X-ray; 2.05 A; A=1-298.
PDB; 1DI8; X-ray; 2.20 A; A=1-298.
PDB; 1DM2; X-ray; 2.10 A; A=1-298.
PDB; 1E1V; X-ray; 1.95 A; A=1-298.
PDB; 1E1X; X-ray; 1.85 A; A=1-298.
PDB; 1E9H; X-ray; 2.50 A; A/C=1-296.
PDB; 1F5Q; X-ray; 2.50 A; A/C=1-298.
PDB; 1FIN; X-ray; 2.30 A; A/C=1-298.
PDB; 1FQ1; X-ray; 3.00 A; B=1-298.
PDB; 1FVT; X-ray; 2.20 A; A=1-298.
PDB; 1FVV; X-ray; 2.80 A; A/C=1-298.
PDB; 1G5S; X-ray; 2.61 A; A=1-298.
PDB; 1GIH; X-ray; 2.80 A; A=1-298.
PDB; 1GII; X-ray; 2.00 A; A=1-298.
PDB; 1GIJ; X-ray; 2.20 A; A=1-298.
PDB; 1GY3; X-ray; 2.70 A; A/C=1-296.
PDB; 1GZ8; X-ray; 1.30 A; A=1-298.
PDB; 1H00; X-ray; 1.60 A; A=1-298.
PDB; 1H01; X-ray; 1.79 A; A=1-298.
PDB; 1H07; X-ray; 1.85 A; A=1-298.
PDB; 1H08; X-ray; 1.80 A; A=1-298.
PDB; 1H0V; X-ray; 1.90 A; A=1-298.
PDB; 1H0W; X-ray; 2.10 A; A=1-298.
PDB; 1H1P; X-ray; 2.10 A; A/C=1-298.
PDB; 1H1Q; X-ray; 2.50 A; A/C=1-298.
PDB; 1H1R; X-ray; 2.00 A; A/C=1-298.
PDB; 1H1S; X-ray; 2.00 A; A/C=1-298.
PDB; 1H24; X-ray; 2.50 A; A/C=1-298.
PDB; 1H25; X-ray; 2.50 A; A/C=1-298.
PDB; 1H26; X-ray; 2.24 A; A/C=1-298.
PDB; 1H27; X-ray; 2.20 A; A/C=1-298.
PDB; 1H28; X-ray; 2.80 A; A/C=1-298.
PDB; 1HCK; X-ray; 1.90 A; A=1-298.
PDB; 1HCL; X-ray; 1.80 A; A=1-298.
PDB; 1JST; X-ray; 2.60 A; A/C=1-298.
PDB; 1JSU; X-ray; 2.30 A; A=1-298.
PDB; 1JSV; X-ray; 1.96 A; A=1-298.
PDB; 1JVP; X-ray; 1.53 A; P=1-298.
PDB; 1KE5; X-ray; 2.20 A; A=1-298.
PDB; 1KE6; X-ray; 2.00 A; A=1-298.
PDB; 1KE7; X-ray; 2.00 A; A=1-298.
PDB; 1KE8; X-ray; 2.00 A; A=1-298.
PDB; 1KE9; X-ray; 2.00 A; A=1-298.
PDB; 1OGU; X-ray; 2.60 A; A/C=1-298.
PDB; 1OI9; X-ray; 2.10 A; A/C=1-298.
PDB; 1OIQ; X-ray; 2.31 A; A=1-298.
PDB; 1OIR; X-ray; 1.91 A; A=1-298.
PDB; 1OIT; X-ray; 1.60 A; A=1-298.
PDB; 1OIU; X-ray; 2.00 A; A/C=1-298.
PDB; 1OIY; X-ray; 2.40 A; A/C=1-298.
PDB; 1OKV; X-ray; 2.40 A; A/C=1-298.
PDB; 1OKW; X-ray; 2.50 A; A/C=1-298.
PDB; 1OL1; X-ray; 2.90 A; A/C=1-298.
PDB; 1OL2; X-ray; 2.60 A; A/C=1-298.
PDB; 1P2A; X-ray; 2.50 A; A=1-298.
PDB; 1P5E; X-ray; 2.22 A; A/C=1-298.
PDB; 1PF8; X-ray; 2.51 A; A=1-298.
PDB; 1PKD; X-ray; 2.30 A; A/C=1-296.
PDB; 1PW2; X-ray; 1.95 A; A=1-298.
PDB; 1PXI; X-ray; 1.95 A; A=1-298.
PDB; 1PXJ; X-ray; 2.30 A; A=1-298.
PDB; 1PXK; X-ray; 2.80 A; A=1-298.
PDB; 1PXL; X-ray; 2.50 A; A=1-298.
PDB; 1PXM; X-ray; 2.53 A; A=1-298.
PDB; 1PXN; X-ray; 2.50 A; A=1-298.
PDB; 1PXO; X-ray; 1.96 A; A=1-298.
PDB; 1PXP; X-ray; 2.30 A; A=1-298.
PDB; 1PYE; X-ray; 2.00 A; A=1-298.
PDB; 1QMZ; X-ray; 2.20 A; A/C=1-298.
PDB; 1R78; X-ray; 2.00 A; A=1-298.
PDB; 1URC; X-ray; 2.60 A; A/C=1-298.
PDB; 1URW; X-ray; 1.60 A; A=1-298.
PDB; 1V1K; X-ray; 2.31 A; A=1-298.
PDB; 1VYW; X-ray; 2.30 A; A/C=1-298.
PDB; 1VYZ; X-ray; 2.21 A; A=1-298.
PDB; 1W0X; X-ray; 2.20 A; C=1-298.
PDB; 1W8C; X-ray; 2.05 A; A=1-298.
PDB; 1W98; X-ray; 2.15 A; A=1-297.
PDB; 1WCC; X-ray; 2.20 A; A=1-298.
PDB; 1Y8Y; X-ray; 2.00 A; A=1-298.
PDB; 1Y91; X-ray; 2.15 A; A=1-298.
PDB; 1YKR; X-ray; 1.80 A; A=1-298.
PDB; 2A0C; X-ray; 1.95 A; X=1-298.
PDB; 2A4L; X-ray; 2.40 A; A=1-298.
PDB; 2B52; X-ray; 1.88 A; A=1-298.
PDB; 2B53; X-ray; 2.00 A; A=1-298.
PDB; 2B54; X-ray; 1.85 A; A=1-298.
PDB; 2B55; X-ray; 1.85 A; A=1-298.
PDB; 2BHE; X-ray; 1.90 A; A=1-298.
PDB; 2BHH; X-ray; 2.60 A; A=1-298.
PDB; 2BKZ; X-ray; 2.60 A; A/C=1-298.
PDB; 2BPM; X-ray; 2.40 A; A/C=1-298.
PDB; 2BTR; X-ray; 1.85 A; A=1-298.
PDB; 2BTS; X-ray; 1.99 A; A=1-298.
PDB; 2C4G; X-ray; 2.70 A; A/C=1-298.
PDB; 2C5N; X-ray; 2.10 A; A/C=1-298.
PDB; 2C5O; X-ray; 2.10 A; A/C=1-298.
PDB; 2C5V; X-ray; 2.90 A; A/C=1-298.
PDB; 2C5X; X-ray; 2.90 A; A/C=1-298.
PDB; 2C5Y; X-ray; 2.25 A; A=1-298.
PDB; 2C68; X-ray; 1.95 A; A=1-298.
PDB; 2C69; X-ray; 2.10 A; A=1-298.
PDB; 2C6I; X-ray; 1.80 A; A=1-298.
PDB; 2C6K; X-ray; 1.90 A; A=1-298.
PDB; 2C6L; X-ray; 2.30 A; A=1-298.
PDB; 2C6M; X-ray; 1.90 A; A=1-298.
PDB; 2C6O; X-ray; 2.10 A; A=1-298.
PDB; 2C6T; X-ray; 2.61 A; A/C=1-298.
PDB; 2CCH; X-ray; 1.70 A; A/C=1-298.
PDB; 2CCI; X-ray; 2.70 A; A/C=1-298.
PDB; 2CJM; X-ray; 2.30 A; A/C=1-298.
PDB; 2CLX; X-ray; 1.80 A; A=1-298.
PDB; 2DS1; X-ray; 2.00 A; A=1-298.
PDB; 2DUV; X-ray; 2.20 A; A=1-298.
PDB; 2EXM; X-ray; 1.80 A; A=1-298.
PDB; 2FVD; X-ray; 1.85 A; A=1-298.
PDB; 2G9X; X-ray; 2.50 A; A/C=1-298.
PDB; 2HIC; Model; -; A=1-298.
PDB; 2I40; X-ray; 2.80 A; A/C=1-298.
PDB; 2IW6; X-ray; 2.30 A; A/C=1-298.
PDB; 2IW8; X-ray; 2.30 A; A/C=1-298.
PDB; 2IW9; X-ray; 2.00 A; A/C=1-298.
PDB; 2J9M; X-ray; 2.50 A; A=1-298.
PDB; 2JGZ; X-ray; 2.90 A; A=1-288.
PDB; 2R3F; X-ray; 1.50 A; A=1-298.
PDB; 2R3G; X-ray; 1.55 A; A=1-298.
PDB; 2R3H; X-ray; 1.50 A; A=1-298.
PDB; 2R3I; X-ray; 1.28 A; A=1-298.
PDB; 2R3J; X-ray; 1.65 A; A=1-298.
PDB; 2R3K; X-ray; 1.70 A; A=1-298.
PDB; 2R3L; X-ray; 1.65 A; A=1-298.
PDB; 2R3M; X-ray; 1.70 A; A=1-298.
PDB; 2R3N; X-ray; 1.63 A; A=1-298.
PDB; 2R3O; X-ray; 1.80 A; A=1-298.
PDB; 2R3P; X-ray; 1.66 A; A=1-298.
PDB; 2R3Q; X-ray; 1.35 A; A=1-298.
PDB; 2R3R; X-ray; 1.47 A; A=1-298.
PDB; 2R64; X-ray; 2.30 A; A=1-298.
PDB; 2UUE; X-ray; 2.06 A; A/C=1-298.
PDB; 2UZB; X-ray; 2.70 A; A/C=1-298.
PDB; 2UZD; X-ray; 2.72 A; A/C=1-298.
PDB; 2UZE; X-ray; 2.40 A; A/C=1-298.
PDB; 2UZL; X-ray; 2.40 A; A/C=1-298.
PDB; 2UZN; X-ray; 2.30 A; A=1-298.
PDB; 2UZO; X-ray; 2.30 A; A=1-298.
PDB; 2V0D; X-ray; 2.20 A; A=1-298.
PDB; 2V22; X-ray; 2.60 A; A/C=1-298.
PDB; 2VTA; X-ray; 2.00 A; A=1-298.
PDB; 2VTH; X-ray; 1.90 A; A=1-298.
PDB; 2VTI; X-ray; 2.00 A; A=1-298.
PDB; 2VTJ; X-ray; 2.20 A; A=1-298.
PDB; 2VTL; X-ray; 2.00 A; A=1-298.
PDB; 2VTM; X-ray; 2.25 A; A=1-298.
PDB; 2VTN; X-ray; 2.20 A; A=1-298.
PDB; 2VTO; X-ray; 2.19 A; A=1-298.
PDB; 2VTP; X-ray; 2.15 A; A=1-298.
PDB; 2VTQ; X-ray; 1.90 A; A=1-298.
PDB; 2VTR; X-ray; 1.90 A; A=1-298.
PDB; 2VTS; X-ray; 1.90 A; A=1-298.
PDB; 2VTT; X-ray; 1.68 A; A=1-298.
PDB; 2VU3; X-ray; 1.85 A; A=1-298.
PDB; 2VV9; X-ray; 1.90 A; A=1-298.
PDB; 2W05; X-ray; 1.90 A; A=1-298.
PDB; 2W06; X-ray; 2.04 A; A=1-298.
PDB; 2W17; X-ray; 2.15 A; A=1-298.
PDB; 2W1H; X-ray; 2.15 A; A=1-298.
PDB; 2WEV; X-ray; 2.30 A; A/C=1-298.
PDB; 2WFY; X-ray; 2.53 A; A/C=1-298.
PDB; 2WHB; X-ray; 2.90 A; A/C=1-298.
PDB; 2WIH; X-ray; 2.50 A; A/C=1-298.
PDB; 2WIP; X-ray; 2.80 A; A/C=1-298.
PDB; 2WMA; X-ray; 2.80 A; A/C=1-298.
PDB; 2WMB; X-ray; 2.60 A; A/C=1-298.
PDB; 2WPA; X-ray; 2.51 A; A/C=1-298.
PDB; 2WXV; X-ray; 2.60 A; A/C=1-298.
PDB; 2X1N; X-ray; 2.75 A; A/C=1-298.
PDB; 2XMY; X-ray; 1.90 A; A=1-298.
PDB; 2XNB; X-ray; 1.85 A; A=1-298.
PDB; 3BHT; X-ray; 2.00 A; A/C=1-298.
PDB; 3BHU; X-ray; 2.30 A; A/C=1-298.
PDB; 3BHV; X-ray; 2.10 A; A/C=1-298.
PDB; 3DDP; X-ray; 2.70 A; A/C=1-298.
PDB; 3DDQ; X-ray; 1.80 A; A/C=1-298.
PDB; 3DOG; X-ray; 2.70 A; A/C=1-298.
PDB; 3EID; X-ray; 3.15 A; A/C=1-298.
PDB; 3EJ1; X-ray; 3.22 A; A/C=1-298.
PDB; 3EOC; X-ray; 3.20 A; A/C=1-298.
PDB; 3EZR; X-ray; 1.90 A; A=1-298.
PDB; 3EZV; X-ray; 1.99 A; A=1-298.
PDB; 3F5X; X-ray; 2.40 A; A/C=1-298.
PDB; 3FZ1; X-ray; 1.90 A; A=1-298.
PDB; 3IG7; X-ray; 1.80 A; A=1-298.
PDB; 3IGG; X-ray; 1.80 A; A=1-298.
PDB; 3LE6; X-ray; 2.00 A; A=1-298.
PDB; 3LFN; X-ray; 2.28 A; A=1-298.
PDB; 3LFQ; X-ray; 2.03 A; A=1-298.
PDB; 3LFS; X-ray; 2.40 A; A=1-298.
PDB; 3MY5; X-ray; 2.10 A; A/C=1-298.
PDB; 3NS9; X-ray; 1.78 A; A=1-298.
PDB; 3PJ8; X-ray; 1.96 A; A=1-298.
PDB; 3PXF; X-ray; 1.80 A; A=1-298.
PDB; 3PXQ; X-ray; 1.90 A; A=1-298.
PDB; 3PXR; X-ray; 2.00 A; A=1-298.
PDB; 3PXY; X-ray; 1.80 A; A=1-298.
PDB; 3PXZ; X-ray; 1.70 A; A=1-298.
PDB; 3PY0; X-ray; 1.75 A; A=1-298.
PDB; 3PY1; X-ray; 2.05 A; A=1-298.
PDB; 3QHR; X-ray; 2.17 A; A/C=1-296.
PDB; 3QHW; X-ray; 1.91 A; A/C=1-296.
PDB; 3QL8; X-ray; 1.90 A; A=1-298.
PDB; 3QQF; X-ray; 1.75 A; A=1-298.
PDB; 3QQG; X-ray; 1.90 A; A=1-298.
PDB; 3QQH; X-ray; 1.87 A; A=1-298.
PDB; 3QQJ; X-ray; 1.70 A; A=1-298.
PDB; 3QQK; X-ray; 1.86 A; A=1-298.
PDB; 3QQL; X-ray; 1.85 A; A=1-298.
PDB; 3QRT; X-ray; 1.75 A; A=1-298.
PDB; 3QRU; X-ray; 1.95 A; A=1-298.
PDB; 3QTQ; X-ray; 1.80 A; A=1-298.
PDB; 3QTR; X-ray; 1.85 A; A=1-298.
PDB; 3QTS; X-ray; 1.90 A; A=1-298.
PDB; 3QTU; X-ray; 1.82 A; A=1-298.
PDB; 3QTW; X-ray; 1.85 A; A=1-298.
PDB; 3QTX; X-ray; 1.95 A; A=1-298.
PDB; 3QTZ; X-ray; 2.00 A; A=1-298.
PDB; 3QU0; X-ray; 1.95 A; A=1-298.
PDB; 3QWJ; X-ray; 1.75 A; A=1-298.
PDB; 3QWK; X-ray; 1.85 A; A=1-298.
PDB; 3QX2; X-ray; 1.75 A; A=1-298.
PDB; 3QX4; X-ray; 1.92 A; A=1-298.
PDB; 3QXO; X-ray; 1.75 A; A=1-298.
PDB; 3QXP; X-ray; 1.75 A; A=1-298.
PDB; 3QZF; X-ray; 2.00 A; A=1-298.
PDB; 3QZG; X-ray; 1.75 A; A=1-298.
PDB; 3QZH; X-ray; 1.95 A; A=1-298.
PDB; 3QZI; X-ray; 1.75 A; A=1-298.
PDB; 3R1Q; X-ray; 1.85 A; A=1-298.
PDB; 3R1S; X-ray; 1.80 A; A=1-298.
PDB; 3R1Y; X-ray; 1.80 A; A=1-298.
PDB; 3R28; X-ray; 1.75 A; A=1-298.
PDB; 3R6X; X-ray; 1.75 A; A=1-298.
PDB; 3R71; X-ray; 1.75 A; A=1-298.
PDB; 3R73; X-ray; 1.70 A; A=1-298.
PDB; 3R7E; X-ray; 1.90 A; A=1-298.
PDB; 3R7I; X-ray; 1.85 A; A=1-298.
PDB; 3R7U; X-ray; 1.75 A; A=1-298.
PDB; 3R7V; X-ray; 1.95 A; A=1-298.
PDB; 3R7Y; X-ray; 1.90 A; A=1-298.
PDB; 3R83; X-ray; 1.75 A; A=1-298.
PDB; 3R8L; X-ray; 1.90 A; A=1-298.
PDB; 3R8M; X-ray; 1.80 A; A=1-298.
PDB; 3R8P; X-ray; 1.80 A; A=1-298.
PDB; 3R8U; X-ray; 2.00 A; A=1-298.
PDB; 3R8V; X-ray; 1.90 A; A=1-298.
PDB; 3R8Z; X-ray; 1.85 A; A=1-298.
PDB; 3R9D; X-ray; 1.95 A; A=1-298.
PDB; 3R9H; X-ray; 2.10 A; A=1-298.
PDB; 3R9N; X-ray; 1.75 A; A=1-298.
PDB; 3R9O; X-ray; 1.90 A; A=1-298.
PDB; 3RAH; X-ray; 1.75 A; A=1-298.
PDB; 3RAI; X-ray; 1.70 A; A=1-298.
PDB; 3RAK; X-ray; 1.75 A; A=1-298.
PDB; 3RAL; X-ray; 1.75 A; A=1-298.
PDB; 3RJC; X-ray; 1.85 A; A=1-298.
PDB; 3RK5; X-ray; 2.00 A; A=1-298.
PDB; 3RK7; X-ray; 1.80 A; A=1-298.
PDB; 3RK9; X-ray; 1.85 A; A=1-298.
PDB; 3RKB; X-ray; 2.00 A; A=1-298.
PDB; 3RM6; X-ray; 1.60 A; A=1-298.
PDB; 3RM7; X-ray; 1.85 A; A=1-298.
PDB; 3RMF; X-ray; 1.75 A; A=1-298.
PDB; 3RNI; X-ray; 1.95 A; A=1-298.
PDB; 3ROY; X-ray; 1.75 A; A=1-298.
PDB; 3RPO; X-ray; 1.75 A; A=1-298.
PDB; 3RPR; X-ray; 1.75 A; A=1-298.
PDB; 3RPV; X-ray; 1.80 A; A=1-298.
PDB; 3RPY; X-ray; 1.90 A; A=1-298.
PDB; 3RZB; X-ray; 1.90 A; A=1-298.
PDB; 3S00; X-ray; 1.80 A; A=1-298.
PDB; 3S0O; X-ray; 2.00 A; A=1-298.
PDB; 3S1H; X-ray; 1.75 A; A=1-298.
PDB; 3S2P; X-ray; 2.30 A; A=1-298.
PDB; 3SQQ; X-ray; 1.85 A; A=1-298.
PDB; 3SW4; X-ray; 1.70 A; A=1-298.
PDB; 3SW7; X-ray; 1.80 A; A=1-298.
PDB; 3TI1; X-ray; 1.99 A; A=1-298.
PDB; 3TIY; X-ray; 1.84 A; A=1-298.
PDB; 3TIZ; X-ray; 2.02 A; A=1-298.
PDB; 3TNW; X-ray; 2.00 A; A/C=1-298.
PDB; 3ULI; X-ray; 2.00 A; A=1-298.
PDB; 3UNJ; X-ray; 1.90 A; A=1-298.
PDB; 3UNK; X-ray; 2.10 A; A=1-298.
PDB; 3WBL; X-ray; 2.00 A; A=1-298.
PDB; 4ACM; X-ray; 1.63 A; A=1-298.
PDB; 4BCK; X-ray; 2.05 A; A/C=1-298.
PDB; 4BCM; X-ray; 2.45 A; A/C=1-298.
PDB; 4BCN; X-ray; 2.10 A; A/C=1-298.
PDB; 4BCO; X-ray; 2.05 A; A/C=1-298.
PDB; 4BCP; X-ray; 2.26 A; A/C=1-298.
PDB; 4BCQ; X-ray; 2.40 A; A/C=1-298.
PDB; 4BGH; X-ray; 1.95 A; A=1-298.
PDB; 4BZD; X-ray; 1.83 A; A=1-298.
PDB; 4CFM; X-ray; 2.85 A; A/C=1-298.
PDB; 4CFN; X-ray; 2.20 A; A/C=1-298.
PDB; 4CFU; X-ray; 2.20 A; A/C=1-298.
PDB; 4CFV; X-ray; 2.00 A; A/C=1-298.
PDB; 4CFW; X-ray; 2.45 A; A/C=1-298.
PDB; 4CFX; X-ray; 3.50 A; A/C=1-298.
PDB; 4D1X; X-ray; 2.10 A; A=1-298.
PDB; 4D1Z; X-ray; 1.85 A; A=1-298.
PDB; 4EK3; X-ray; 1.34 A; A=1-298.
PDB; 4EK4; X-ray; 1.26 A; A=1-298.
PDB; 4EK5; X-ray; 1.60 A; A=1-298.
PDB; 4EK6; X-ray; 1.52 A; A=1-298.
PDB; 4EK8; X-ray; 1.70 A; A=1-298.
PDB; 4EOI; X-ray; 2.00 A; A/C=1-298.
PDB; 4EOJ; X-ray; 1.65 A; A/C=1-298.
PDB; 4EOK; X-ray; 2.57 A; A/C=1-297.
PDB; 4EOL; X-ray; 2.40 A; A/C=1-297.
PDB; 4EOM; X-ray; 2.10 A; A/C=1-297.
PDB; 4EON; X-ray; 2.40 A; A/C=1-298.
PDB; 4EOO; X-ray; 2.10 A; A/C=1-297.
PDB; 4EOP; X-ray; 1.99 A; A/C=1-297.
PDB; 4EOQ; X-ray; 2.15 A; A/C=1-297.
PDB; 4EOR; X-ray; 2.20 A; A/C=1-297.
PDB; 4EOS; X-ray; 2.57 A; A/C=1-297.
PDB; 4ERW; X-ray; 2.00 A; A=1-298.
PDB; 4EZ3; X-ray; 2.00 A; A=1-298.
PDB; 4EZ7; X-ray; 2.49 A; A=1-298.
PDB; 4FKG; X-ray; 1.51 A; A=1-298.
PDB; 4FKI; X-ray; 1.60 A; A=1-298.
PDB; 4FKJ; X-ray; 1.63 A; A=1-298.
PDB; 4FKL; X-ray; 1.26 A; A=1-298.
PDB; 4FKO; X-ray; 1.55 A; A=1-298.
PDB; 4FKP; X-ray; 1.60 A; A=1-298.
PDB; 4FKQ; X-ray; 1.75 A; A=1-298.
PDB; 4FKR; X-ray; 1.90 A; A=1-298.
PDB; 4FKS; X-ray; 1.55 A; A=1-298.
PDB; 4FKT; X-ray; 1.60 A; A=1-298.
PDB; 4FKU; X-ray; 1.47 A; A=1-298.
PDB; 4FKV; X-ray; 1.70 A; A=1-298.
PDB; 4FKW; X-ray; 1.80 A; A=1-298.
PDB; 4FX3; X-ray; 2.75 A; A/C=1-298.
PDB; 4GCJ; X-ray; 1.42 A; A=1-298.
PDB; 4I3Z; X-ray; 2.05 A; A/C=1-296.
PDB; 4II5; X-ray; 2.15 A; A/C=1-298.
PDB; 4KD1; X-ray; 1.70 A; A=1-298.
PDB; 4LYN; X-ray; 2.00 A; A=1-298.
PDB; 4NJ3; X-ray; 1.85 A; A=1-298.
PDB; 4RJ3; X-ray; 1.63 A; A=1-298.
PDB; 5A14; X-ray; 2.00 A; A=1-298.
PDB; 5AND; X-ray; 2.30 A; A=1-298.
PDB; 5ANE; X-ray; 1.70 A; A=1-298.
PDB; 5ANG; X-ray; 1.90 A; A=1-298.
PDB; 5ANI; X-ray; 1.90 A; A=1-298.
PDB; 5ANJ; X-ray; 1.60 A; A=1-298.
PDB; 5ANK; X-ray; 1.90 A; A=1-298.
PDB; 5ANO; X-ray; 1.70 A; A=1-298.
PDB; 5CYI; X-ray; 2.00 A; A/C=1-298.
PDB; 5D1J; X-ray; 1.80 A; A=1-298.
PDB; 5FP5; X-ray; 2.16 A; A=1-298.
PDB; 5FP6; X-ray; 1.85 A; A=1-298.
PDB; 5IEV; X-ray; 2.03 A; A=1-298.
PDB; 5IEX; X-ray; 2.03 A; A=1-298.
PDB; 5IEY; X-ray; 1.66 A; A=1-298.
PDB; 5IF1; X-ray; 2.61 A; A/C=1-298.
PDB; 5JQ5; X-ray; 1.94 A; A=1-298.
PDB; 5JQ8; X-ray; 1.94 A; A=1-298.
PDB; 5K4J; X-ray; 1.60 A; A=1-298.
PDB; 5L2W; X-ray; 2.80 A; A=1-298.
PDB; 5LMK; X-ray; 2.40 A; A=1-298, C=1-296.
PDB; 5NEV; X-ray; 2.97 A; A/C=1-298.
PDB; 5UQ1; X-ray; 3.20 A; A/C=1-298.
PDB; 5UQ2; X-ray; 2.70 A; A=1-298.
PDB; 5UQ3; X-ray; 3.60 A; A=1-298.
PDBsum; 1AQ1; -.
PDBsum; 1B38; -.
PDBsum; 1B39; -.
PDBsum; 1BUH; -.
PDBsum; 1CKP; -.
PDBsum; 1DI8; -.
PDBsum; 1DM2; -.
PDBsum; 1E1V; -.
PDBsum; 1E1X; -.
PDBsum; 1E9H; -.
PDBsum; 1F5Q; -.
PDBsum; 1FIN; -.
PDBsum; 1FQ1; -.
PDBsum; 1FVT; -.
PDBsum; 1FVV; -.
PDBsum; 1G5S; -.
PDBsum; 1GIH; -.
PDBsum; 1GII; -.
PDBsum; 1GIJ; -.
PDBsum; 1GY3; -.
PDBsum; 1GZ8; -.
PDBsum; 1H00; -.
PDBsum; 1H01; -.
PDBsum; 1H07; -.
PDBsum; 1H08; -.
PDBsum; 1H0V; -.
PDBsum; 1H0W; -.
PDBsum; 1H1P; -.
PDBsum; 1H1Q; -.
PDBsum; 1H1R; -.
PDBsum; 1H1S; -.
PDBsum; 1H24; -.
PDBsum; 1H25; -.
PDBsum; 1H26; -.
PDBsum; 1H27; -.
PDBsum; 1H28; -.
PDBsum; 1HCK; -.
PDBsum; 1HCL; -.
PDBsum; 1JST; -.
PDBsum; 1JSU; -.
PDBsum; 1JSV; -.
PDBsum; 1JVP; -.
PDBsum; 1KE5; -.
PDBsum; 1KE6; -.
PDBsum; 1KE7; -.
PDBsum; 1KE8; -.
PDBsum; 1KE9; -.
PDBsum; 1OGU; -.
PDBsum; 1OI9; -.
PDBsum; 1OIQ; -.
PDBsum; 1OIR; -.
PDBsum; 1OIT; -.
PDBsum; 1OIU; -.
PDBsum; 1OIY; -.
PDBsum; 1OKV; -.
PDBsum; 1OKW; -.
PDBsum; 1OL1; -.
PDBsum; 1OL2; -.
PDBsum; 1P2A; -.
PDBsum; 1P5E; -.
PDBsum; 1PF8; -.
PDBsum; 1PKD; -.
PDBsum; 1PW2; -.
PDBsum; 1PXI; -.
PDBsum; 1PXJ; -.
PDBsum; 1PXK; -.
PDBsum; 1PXL; -.
PDBsum; 1PXM; -.
PDBsum; 1PXN; -.
PDBsum; 1PXO; -.
PDBsum; 1PXP; -.
PDBsum; 1PYE; -.
PDBsum; 1QMZ; -.
PDBsum; 1R78; -.
PDBsum; 1URC; -.
PDBsum; 1URW; -.
PDBsum; 1V1K; -.
PDBsum; 1VYW; -.
PDBsum; 1VYZ; -.
PDBsum; 1W0X; -.
PDBsum; 1W8C; -.
PDBsum; 1W98; -.
PDBsum; 1WCC; -.
PDBsum; 1Y8Y; -.
PDBsum; 1Y91; -.
PDBsum; 1YKR; -.
PDBsum; 2A0C; -.
PDBsum; 2A4L; -.
PDBsum; 2B52; -.
PDBsum; 2B53; -.
PDBsum; 2B54; -.
PDBsum; 2B55; -.
PDBsum; 2BHE; -.
PDBsum; 2BHH; -.
PDBsum; 2BKZ; -.
PDBsum; 2BPM; -.
PDBsum; 2BTR; -.
PDBsum; 2BTS; -.
PDBsum; 2C4G; -.
PDBsum; 2C5N; -.
PDBsum; 2C5O; -.
PDBsum; 2C5V; -.
PDBsum; 2C5X; -.
PDBsum; 2C5Y; -.
PDBsum; 2C68; -.
PDBsum; 2C69; -.
PDBsum; 2C6I; -.
PDBsum; 2C6K; -.
PDBsum; 2C6L; -.
PDBsum; 2C6M; -.
PDBsum; 2C6O; -.
PDBsum; 2C6T; -.
PDBsum; 2CCH; -.
PDBsum; 2CCI; -.
PDBsum; 2CJM; -.
PDBsum; 2CLX; -.
PDBsum; 2DS1; -.
PDBsum; 2DUV; -.
PDBsum; 2EXM; -.
PDBsum; 2FVD; -.
PDBsum; 2G9X; -.
PDBsum; 2HIC; -.
PDBsum; 2I40; -.
PDBsum; 2IW6; -.
PDBsum; 2IW8; -.
PDBsum; 2IW9; -.
PDBsum; 2J9M; -.
PDBsum; 2JGZ; -.
PDBsum; 2R3F; -.
PDBsum; 2R3G; -.
PDBsum; 2R3H; -.
PDBsum; 2R3I; -.
PDBsum; 2R3J; -.
PDBsum; 2R3K; -.
PDBsum; 2R3L; -.
PDBsum; 2R3M; -.
PDBsum; 2R3N; -.
PDBsum; 2R3O; -.
PDBsum; 2R3P; -.
PDBsum; 2R3Q; -.
PDBsum; 2R3R; -.
PDBsum; 2R64; -.
PDBsum; 2UUE; -.
PDBsum; 2UZB; -.
PDBsum; 2UZD; -.
PDBsum; 2UZE; -.
PDBsum; 2UZL; -.
PDBsum; 2UZN; -.
PDBsum; 2UZO; -.
PDBsum; 2V0D; -.
PDBsum; 2V22; -.
PDBsum; 2VTA; -.
PDBsum; 2VTH; -.
PDBsum; 2VTI; -.
PDBsum; 2VTJ; -.
PDBsum; 2VTL; -.
PDBsum; 2VTM; -.
PDBsum; 2VTN; -.
PDBsum; 2VTO; -.
PDBsum; 2VTP; -.
PDBsum; 2VTQ; -.
PDBsum; 2VTR; -.
PDBsum; 2VTS; -.
PDBsum; 2VTT; -.
PDBsum; 2VU3; -.
PDBsum; 2VV9; -.
PDBsum; 2W05; -.
PDBsum; 2W06; -.
PDBsum; 2W17; -.
PDBsum; 2W1H; -.
PDBsum; 2WEV; -.
PDBsum; 2WFY; -.
PDBsum; 2WHB; -.
PDBsum; 2WIH; -.
PDBsum; 2WIP; -.
PDBsum; 2WMA; -.
PDBsum; 2WMB; -.
PDBsum; 2WPA; -.
PDBsum; 2WXV; -.
PDBsum; 2X1N; -.
PDBsum; 2XMY; -.
PDBsum; 2XNB; -.
PDBsum; 3BHT; -.
PDBsum; 3BHU; -.
PDBsum; 3BHV; -.
PDBsum; 3DDP; -.
PDBsum; 3DDQ; -.
PDBsum; 3DOG; -.
PDBsum; 3EID; -.
PDBsum; 3EJ1; -.
PDBsum; 3EOC; -.
PDBsum; 3EZR; -.
PDBsum; 3EZV; -.
PDBsum; 3F5X; -.
PDBsum; 3FZ1; -.
PDBsum; 3IG7; -.
PDBsum; 3IGG; -.
PDBsum; 3LE6; -.
PDBsum; 3LFN; -.
PDBsum; 3LFQ; -.
PDBsum; 3LFS; -.
PDBsum; 3MY5; -.
PDBsum; 3NS9; -.
PDBsum; 3PJ8; -.
PDBsum; 3PXF; -.
PDBsum; 3PXQ; -.
PDBsum; 3PXR; -.
PDBsum; 3PXY; -.
PDBsum; 3PXZ; -.
PDBsum; 3PY0; -.
PDBsum; 3PY1; -.
PDBsum; 3QHR; -.
PDBsum; 3QHW; -.
PDBsum; 3QL8; -.
PDBsum; 3QQF; -.
PDBsum; 3QQG; -.
PDBsum; 3QQH; -.
PDBsum; 3QQJ; -.
PDBsum; 3QQK; -.
PDBsum; 3QQL; -.
PDBsum; 3QRT; -.
PDBsum; 3QRU; -.
PDBsum; 3QTQ; -.
PDBsum; 3QTR; -.
PDBsum; 3QTS; -.
PDBsum; 3QTU; -.
PDBsum; 3QTW; -.
PDBsum; 3QTX; -.
PDBsum; 3QTZ; -.
PDBsum; 3QU0; -.
PDBsum; 3QWJ; -.
PDBsum; 3QWK; -.
PDBsum; 3QX2; -.
PDBsum; 3QX4; -.
PDBsum; 3QXO; -.
PDBsum; 3QXP; -.
PDBsum; 3QZF; -.
PDBsum; 3QZG; -.
PDBsum; 3QZH; -.
PDBsum; 3QZI; -.
PDBsum; 3R1Q; -.
PDBsum; 3R1S; -.
PDBsum; 3R1Y; -.
PDBsum; 3R28; -.
PDBsum; 3R6X; -.
PDBsum; 3R71; -.
PDBsum; 3R73; -.
PDBsum; 3R7E; -.
PDBsum; 3R7I; -.
PDBsum; 3R7U; -.
PDBsum; 3R7V; -.
PDBsum; 3R7Y; -.
PDBsum; 3R83; -.
PDBsum; 3R8L; -.
PDBsum; 3R8M; -.
PDBsum; 3R8P; -.
PDBsum; 3R8U; -.
PDBsum; 3R8V; -.
PDBsum; 3R8Z; -.
PDBsum; 3R9D; -.
PDBsum; 3R9H; -.
PDBsum; 3R9N; -.
PDBsum; 3R9O; -.
PDBsum; 3RAH; -.
PDBsum; 3RAI; -.
PDBsum; 3RAK; -.
PDBsum; 3RAL; -.
PDBsum; 3RJC; -.
PDBsum; 3RK5; -.
PDBsum; 3RK7; -.
PDBsum; 3RK9; -.
PDBsum; 3RKB; -.
PDBsum; 3RM6; -.
PDBsum; 3RM7; -.
PDBsum; 3RMF; -.
PDBsum; 3RNI; -.
PDBsum; 3ROY; -.
PDBsum; 3RPO; -.
PDBsum; 3RPR; -.
PDBsum; 3RPV; -.
PDBsum; 3RPY; -.
PDBsum; 3RZB; -.
PDBsum; 3S00; -.
PDBsum; 3S0O; -.
PDBsum; 3S1H; -.
PDBsum; 3S2P; -.
PDBsum; 3SQQ; -.
PDBsum; 3SW4; -.
PDBsum; 3SW7; -.
PDBsum; 3TI1; -.
PDBsum; 3TIY; -.
PDBsum; 3TIZ; -.
PDBsum; 3TNW; -.
PDBsum; 3ULI; -.
PDBsum; 3UNJ; -.
PDBsum; 3UNK; -.
PDBsum; 3WBL; -.
PDBsum; 4ACM; -.
PDBsum; 4BCK; -.
PDBsum; 4BCM; -.
PDBsum; 4BCN; -.
PDBsum; 4BCO; -.
PDBsum; 4BCP; -.
PDBsum; 4BCQ; -.
PDBsum; 4BGH; -.
PDBsum; 4BZD; -.
PDBsum; 4CFM; -.
PDBsum; 4CFN; -.
PDBsum; 4CFU; -.
PDBsum; 4CFV; -.
PDBsum; 4CFW; -.
PDBsum; 4CFX; -.
PDBsum; 4D1X; -.
PDBsum; 4D1Z; -.
PDBsum; 4EK3; -.
PDBsum; 4EK4; -.
PDBsum; 4EK5; -.
PDBsum; 4EK6; -.
PDBsum; 4EK8; -.
PDBsum; 4EOI; -.
PDBsum; 4EOJ; -.
PDBsum; 4EOK; -.
PDBsum; 4EOL; -.
PDBsum; 4EOM; -.
PDBsum; 4EON; -.
PDBsum; 4EOO; -.
PDBsum; 4EOP; -.
PDBsum; 4EOQ; -.
PDBsum; 4EOR; -.
PDBsum; 4EOS; -.
PDBsum; 4ERW; -.
PDBsum; 4EZ3; -.
PDBsum; 4EZ7; -.
PDBsum; 4FKG; -.
PDBsum; 4FKI; -.
PDBsum; 4FKJ; -.
PDBsum; 4FKL; -.
PDBsum; 4FKO; -.
PDBsum; 4FKP; -.
PDBsum; 4FKQ; -.
PDBsum; 4FKR; -.
PDBsum; 4FKS; -.
PDBsum; 4FKT; -.
PDBsum; 4FKU; -.
PDBsum; 4FKV; -.
PDBsum; 4FKW; -.
PDBsum; 4FX3; -.
PDBsum; 4GCJ; -.
PDBsum; 4I3Z; -.
PDBsum; 4II5; -.
PDBsum; 4KD1; -.
PDBsum; 4LYN; -.
PDBsum; 4NJ3; -.
PDBsum; 4RJ3; -.
PDBsum; 5A14; -.
PDBsum; 5AND; -.
PDBsum; 5ANE; -.
PDBsum; 5ANG; -.
PDBsum; 5ANI; -.
PDBsum; 5ANJ; -.
PDBsum; 5ANK; -.
PDBsum; 5ANO; -.
PDBsum; 5CYI; -.
PDBsum; 5D1J; -.
PDBsum; 5FP5; -.
PDBsum; 5FP6; -.
PDBsum; 5IEV; -.
PDBsum; 5IEX; -.
PDBsum; 5IEY; -.
PDBsum; 5IF1; -.
PDBsum; 5JQ5; -.
PDBsum; 5JQ8; -.
PDBsum; 5K4J; -.
PDBsum; 5L2W; -.
PDBsum; 5LMK; -.
PDBsum; 5NEV; -.
PDBsum; 5UQ1; -.
PDBsum; 5UQ2; -.
PDBsum; 5UQ3; -.
ProteinModelPortal; P24941; -.
SMR; P24941; -.
BioGrid; 107452; 682.
CORUM; P24941; -.
DIP; DIP-161N; -.
ELM; P24941; -.
IntAct; P24941; 158.
MINT; MINT-96328; -.
STRING; 9606.ENSP00000266970; -.
BindingDB; P24941; -.
ChEMBL; CHEMBL301; -.
DrugBank; DB07054; (2R)-1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENOXY}PROPAN-2-OL.
DrugBank; DB07504; (2R)-1-{4-[(4-ANILINO-5-BROMOPYRIMIDIN-2-YL)AMINO]PHENOXY}-3-(DIMETHYLAMINO)PROPAN-2-OL.
DrugBank; DB08463; (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol.
DrugBank; DB07501; (2S)-1-{4-[(4-ANILINO-5-BROMOPYRIMIDIN-2-YL)AMINO]PHENOXY}-3-(DIMETHYLAMINO)PROPAN-2-OL.
DrugBank; DB07137; (2S)-N-[(3Z)-5-CYCLOPROPYL-3H-PYRAZOL-3-YLIDENE]-2-[4-(2-OXOIMIDAZOLIDIN-1-YL)PHENYL]PROPANAMIDE.
DrugBank; DB08137; (4E)-N-(4-fluorophenyl)-4-[(phenylcarbonyl)imino]-4H-pyrazole-3-carboxamide.
DrugBank; DB02603; 1-Amino-6-Cyclohex-3-Enylmethyloxypurine.
DrugBank; DB04288; 2-[Trans-(4-Aminocyclohexyl)Amino]-6-(Benzyl-Amino)-9-Cyclopentylpurine.
DrugBank; DB02297; 2-Amino-6-Chloropyrazine.
DrugBank; DB06948; 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE.
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.
DrugBank; DB08248; 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE.
DrugBank; DB08309; 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL.
DrugBank; DB02973; 4-(5-Bromo-2-Oxo-2h-Indol-3-Ylazo)-Benzenesulfonamide.
DrugBank; DB08241; 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE.
DrugBank; DB08136; 4-(acetylamino)-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamide.
DrugBank; DB03307; 4-[(6-Amino-4-Pyrimidinyl)Amino]Benzenesulfonamide.
DrugBank; DB08134; 4-[(6-chloropyrazin-2-yl)amino]benzenesulfonamide.
DrugBank; DB04407; 4-[4-(4-Methyl-2-Methylamino-Thiazol-5-Yl)-Pyrimidin-2-Ylamino]-Phenol.
DrugBank; DB07791; 4-{[4-(1-CYCLOPROPYL-2-METHYL-1H-IMIDAZOL-5-YL)PYRIMIDIN-2-YL]AMINO}-N-METHYLBENZENESULFONAMIDE.
DrugBank; DB08572; 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE.
DrugBank; DB07163; 5-[(2-AMINOETHYL)AMINO]-6-FLUORO-3-(1H-PYRROL-2-YL)BENZO[CD]INDOL-2(1H)-ONE.
DrugBank; DB08132; 5-hydroxynaphthalene-1-sulfonamide.
DrugBank; DB02898; 5-{[(2-Amino-9h-Purin-6-Yl)Oxy]Methyl}-2-Pyrrolidinone.
DrugBank; DB07612; 6-(3-AMINOPHENYL)-N-(TERT-BUTYL)-2-(TRIFLUOROMETHYL)QUINAZOLIN-4-AMINE.
DrugBank; DB08247; 6-(CYCLOHEXYLMETHOXY)-8-ISOPROPYL-9H-PURIN-2-AMINE.
DrugBank; DB07203; 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE.
DrugBank; DB08233; 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE.
DrugBank; DB02407; 6-O-Cyclohexylmethyl Guanine.
DrugBank; DB02833; [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine.
DrugBank; DB05037; AT7519.
DrugBank; DB06616; Bosutinib.
DrugBank; DB03496; Flavopiridol.
DrugBank; DB02950; Hymenialdisine.
DrugBank; DB02052; Indirubin-3'-Monoxime.
DrugBank; DB03801; Lysine Nz-Carboxylic Acid.
DrugBank; DB07790; N-(2-METHOXYETHYL)-4-({4-[2-METHYL-1-(1-METHYLETHYL)-1H-IMIDAZOL-5-YL]PYRIMIDIN-2-YL}AMINO)BENZENESULFONAMIDE.
DrugBank; DB06944; N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide.
DrugBank; DB08768; N-(3-METHYLBUT-2-EN-1-YL)-9H-PURIN-6-AMINE.
DrugBank; DB08133; N-(4-sulfamoylphenyl)-1H-indazole-3-carboxamide.
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.
DrugBank; DB02647; N-(5-Cyclopropyl-1h-Pyrazol-3-Yl)Benzamide.
DrugBank; DB08677; N-(5-ISOPROPYL-THIAZOL-2-YL)-2-PYRIDIN-3-YL-ACETAMIDE.
DrugBank; DB08066; N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE.
DrugBank; DB08135; N-phenyl-1H-pyrazole-3-carboxamide.
DrugBank; DB07126; O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE.
DrugBank; DB02116; Olomoucine.
DrugBank; DB04662; OLOMOUCINE II.
DrugBank; DB02733; Purvalanol.
DrugBank; DB02010; Staurosporine.
DrugBank; DB03428; SU9516.
DrugBank; DB04669; TRIAZOLOPYRIMIDINE.
GuidetoPHARMACOLOGY; 1973; -.
iPTMnet; P24941; -.
PhosphoSitePlus; P24941; -.
SwissPalm; P24941; -.
BioMuta; CDK2; -.
DMDM; 116051; -.
EPD; P24941; -.
MaxQB; P24941; -.
PaxDb; P24941; -.
PeptideAtlas; P24941; -.
PRIDE; P24941; -.
DNASU; 1017; -.
Ensembl; ENST00000266970; ENSP00000266970; ENSG00000123374. [P24941-1]
Ensembl; ENST00000354056; ENSP00000243067; ENSG00000123374. [P24941-2]
GeneID; 1017; -.
KEGG; hsa:1017; -.
UCSC; uc001sit.5; human. [P24941-1]
CTD; 1017; -.
DisGeNET; 1017; -.
EuPathDB; HostDB:ENSG00000123374.10; -.
GeneCards; CDK2; -.
HGNC; HGNC:1771; CDK2.
HPA; CAB013115; -.
HPA; HPA066915; -.
MIM; 116953; gene.
neXtProt; NX_P24941; -.
OpenTargets; ENSG00000123374; -.
PharmGKB; PA101; -.
eggNOG; KOG0594; Eukaryota.
eggNOG; ENOG410XPP3; LUCA.
GeneTree; ENSGT00900000140881; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P24941; -.
KO; K02206; -.
PhylomeDB; P24941; -.
TreeFam; TF101021; -.
BRENDA; 2.7.11.22; 2681.
Reactome; R-HSA-1538133; G0 and Early G1.
Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-68911; G2 Phase.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-68962; Activation of the pre-replicative complex.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69563; p53-Dependent G1 DNA Damage Response.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-8849470; PTK6 Regulates Cell Cycle.
Reactome; R-HSA-912446; Meiotic recombination.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P24941; -.
SIGNOR; P24941; -.
ChiTaRS; CDK2; human.
EvolutionaryTrace; P24941; -.
GeneWiki; Cyclin-dependent_kinase_2; -.
GenomeRNAi; 1017; -.
PRO; PR:P24941; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000123374; -.
CleanEx; HS_CDK2; -.
ExpressionAtlas; P24941; baseline and differential.
Genevisible; P24941; HS.
GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; TAS:UniProtKB.
GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
GO; GO:0097123; C:cyclin A1-CDK2 complex; IEA:Ensembl.
GO; GO:0097124; C:cyclin A2-CDK2 complex; IDA:UniProtKB.
GO; GO:0097134; C:cyclin E1-CDK2 complex; IEA:Ensembl.
GO; GO:0097135; C:cyclin E2-CDK2 complex; IEA:Ensembl.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:CAFA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0000805; C:X chromosome; IEA:Ensembl.
GO; GO:0000806; C:Y chromosome; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0030332; F:cyclin binding; IDA:UniProtKB.
GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071732; P:cellular response to nitric oxide; TAS:UniProtKB.
GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
GO; GO:0051298; P:centrosome duplication; TAS:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; TAS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0016572; P:histone phosphorylation; IDA:CAFA.
GO; GO:0051321; P:meiotic cell cycle; TAS:UniProtKB.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; TAS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0032298; P:positive regulation of DNA-dependent DNA replication initiation; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0060968; P:regulation of gene silencing; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0010033; P:response to organic substance; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
DNA damage; DNA repair; Endosome; Kinase; Magnesium; Meiosis;
Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; S-nitrosylation;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 298 Cyclin-dependent kinase 2.
/FTId=PRO_0000085769.
DOMAIN 4 286 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 10 18 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:17095507,
ECO:0000269|PubMed:21565702}.
NP_BIND 81 83 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:17095507,
ECO:0000269|PubMed:21565702}.
NP_BIND 129 132 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:17095507,
ECO:0000269|PubMed:21565702}.
ACT_SITE 127 127 Proton acceptor.
METAL 132 132 Magnesium. {ECO:0000269|PubMed:21565702}.
METAL 145 145 Magnesium. {ECO:0000269|PubMed:21565702}.
BINDING 33 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:17095507,
ECO:0000269|PubMed:21565702}.
BINDING 86 86 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:17095507,
ECO:0000269|PubMed:21565702}.
BINDING 145 145 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:17095507,
ECO:0000269|PubMed:21565702}.
SITE 9 9 CDK7 binding.
SITE 88 89 CDK7 binding.
SITE 166 166 CDK7 binding.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 14 14 Phosphothreonine.
{ECO:0000269|PubMed:1396589,
ECO:0000269|PubMed:17095507}.
MOD_RES 15 15 Phosphotyrosine; by WEE1.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:1396589,
ECO:0000269|PubMed:17095507}.
MOD_RES 19 19 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 160 160 Phosphothreonine; by CAK and CCRK.
{ECO:0000269|PubMed:1396589,
ECO:0000269|PubMed:14597612,
ECO:0000269|PubMed:16325401,
ECO:0000269|PubMed:17095507,
ECO:0000269|PubMed:17570665,
ECO:0000269|PubMed:20147522,
ECO:0000269|PubMed:20360007,
ECO:0000269|PubMed:21565702}.
VAR_SEQ 163 196 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_041998.
VARIANT 15 15 Y -> S (in dbSNP:rs3087335).
/FTId=VAR_016157.
VARIANT 18 18 V -> L (in dbSNP:rs11554376).
/FTId=VAR_053927.
VARIANT 45 45 P -> L (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041972.
VARIANT 290 290 T -> S (in dbSNP:rs2069413).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.6}.
/FTId=VAR_019988.
MUTAGEN 9 9 K->F: Reduced phosphorylation by CAK.
{ECO:0000269|PubMed:17373709}.
MUTAGEN 14 14 T->A: 2-fold increase in activity.
{ECO:0000269|PubMed:1396589}.
MUTAGEN 15 15 Y->F: 2-fold increase in activity.
{ECO:0000269|PubMed:1396589}.
MUTAGEN 88 89 KK->EV: Reduced phosphorylation by CAK.
{ECO:0000269|PubMed:17373709}.
MUTAGEN 160 160 T->A: Abolishes activity.
{ECO:0000269|PubMed:1396589}.
MUTAGEN 166 166 L->R: Reduced phosphorylation by CAK and
reduced kinase activity.
{ECO:0000269|PubMed:17373709}.
CONFLICT 8 12 EKIGE -> AQIGQ (in Ref. 5; BAA32794).
{ECO:0000305}.
CONFLICT 25 29 LTGEV -> STGQM (in Ref. 5; BAA32794).
{ECO:0000305}.
CONFLICT 272 277 NKRISA -> YKRFST (in Ref. 5; BAA32794).
{ECO:0000305}.
CONFLICT 286 287 FQ -> LE (in Ref. 5; BAA32794).
{ECO:0000305}.
HELIX 1 3 {ECO:0000244|PDB:5K4J}.
STRAND 4 12 {ECO:0000244|PDB:4EK4}.
STRAND 14 23 {ECO:0000244|PDB:4EK4}.
TURN 24 26 {ECO:0000244|PDB:4EK4}.
STRAND 29 35 {ECO:0000244|PDB:4EK4}.
STRAND 39 41 {ECO:0000244|PDB:4GCJ}.
STRAND 42 44 {ECO:0000244|PDB:2CCH}.
HELIX 46 54 {ECO:0000244|PDB:4EK4}.
HELIX 55 57 {ECO:0000244|PDB:4EK4}.
STRAND 66 72 {ECO:0000244|PDB:4EK4}.
STRAND 75 81 {ECO:0000244|PDB:4EK4}.
STRAND 84 86 {ECO:0000244|PDB:4EK4}.
HELIX 87 93 {ECO:0000244|PDB:4EK4}.
TURN 94 97 {ECO:0000244|PDB:4EK4}.
HELIX 101 120 {ECO:0000244|PDB:4EK4}.
HELIX 130 132 {ECO:0000244|PDB:4EK4}.
STRAND 133 135 {ECO:0000244|PDB:4EK4}.
TURN 137 139 {ECO:0000244|PDB:2B54}.
STRAND 141 143 {ECO:0000244|PDB:4EK4}.
HELIX 148 152 {ECO:0000244|PDB:4EK4}.
HELIX 156 158 {ECO:0000244|PDB:4FKO}.
STRAND 159 161 {ECO:0000244|PDB:3RAI}.
HELIX 162 168 {ECO:0000244|PDB:4GCJ}.
HELIX 171 174 {ECO:0000244|PDB:4EK4}.
STRAND 178 180 {ECO:0000244|PDB:1OKW}.
HELIX 183 198 {ECO:0000244|PDB:4EK4}.
HELIX 208 219 {ECO:0000244|PDB:4EK4}.
TURN 224 226 {ECO:0000244|PDB:4EK4}.
HELIX 230 232 {ECO:0000244|PDB:4EK4}.
HELIX 248 251 {ECO:0000244|PDB:4EK4}.
STRAND 252 254 {ECO:0000244|PDB:1GY3}.
HELIX 257 266 {ECO:0000244|PDB:4EK4}.
TURN 271 273 {ECO:0000244|PDB:4EK4}.
HELIX 277 281 {ECO:0000244|PDB:4EK4}.
HELIX 284 286 {ECO:0000244|PDB:4EK4}.
TURN 287 289 {ECO:0000244|PDB:1W98}.
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


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