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Database: UniProt/SWISS-PROT
Entry: CDK2_HUMAN
LinkDB: CDK2_HUMAN
Original site: 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   29-OCT-2014, entry version 191.
DE   RecName: Full=Cyclin-dependent kinase 2;
DE            EC=2.7.11.22;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1714386;
RA   Elledge S.J., Spottswood M.R.;
RT   "A new human p34 protein kinase, CDK2, identified by complementation
RT   of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of
RT   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
RT   adenovirus 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
RT   complementation 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
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   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.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   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.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160, AND MUTAGENESIS OF
RP   THR-14; TYR-15 AND THR-160.
RX   PubMed=1396589;
RA   Gu Y., Rosenblatt J., O'Morgan D.O.;
RT   "Cell cycle regulation of CDK2 activity by phosphorylation of Thr160
RT   and Tyr15.";
RL   EMBO J. 11:3995-4005(1992).
RN   [12]
RP   ENZYME 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
RT   selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and
RT   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
RT   that 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.,
RA   Chan P.K., Knudsen E.S., Hofmann I.A., Snyder J.D., Bove K.E.,
RA   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.,
RA   Wang J., Qin J., Chow L.T., Harper J.W.;
RT   "Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2
RT   in 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
RP   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
RT   site 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
RT   by 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.,
RA   Wang X.-Y., Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.;
RT   "Characterization and expression of mammalian cyclin b3, a
RT   prepachytene 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
RT   proliferation 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.,
RA   Donoghue D.J.;
RT   "Human Spy1 promotes survival of mammalian cells following DNA
RT   damage.";
RL   Cancer Res. 63:3701-3707(2003).
RN   [22]
RP   INTERACTION WITH SPDYA, AND IDENTIFICATION IN A COMPLEX WITH CDKN1B
RP   AND 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   [23]
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   [24]
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   [25]
RP   INTERACTION WITH SPDYA AND SPDYC.
RX   PubMed=15611625;
RA   Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.;
RT   "Identification and comparative analysis of multiple mammalian
RT   Speedy/Ringo proteins.";
RL   Cell Cycle 4:155-165(2005).
RN   [26]
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   [27]
RP   PHOSPHORYLATION BY CAK, MUTAGENESIS OF LYS-9; 88-LYS-LYS-89 AND
RP   LEU-166, 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   [28]
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
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [29]
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   [30]
RP   INTERACTION WITH CACUL1.
RX   PubMed=19829063;
RA   Kong Y., Nan K., Yin Y.;
RT   "Identification and characterization of CAC1 as a novel CDK2-
RT   associated cullin.";
RL   Cell Cycle 8:3544-3553(2009).
RN   [31]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, AND IDENTIFICATION
RP   BY 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   [32]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND IDENTIFICATION
RP   BY 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   [33]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-6, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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   [34]
RP   FUNCTION IN VITAMIN D-MEDIATED GROWTH INHIBITION, SUBCELLULAR
RP   LOCATION, ENZYME 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
RT   roles of cyclin-dependent kinase 2 localization and cyclin E in
RT   vitamin D-mediated growth inhibition.";
RL   Endocrinology 151:896-908(2010).
RN   [35]
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   [36]
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
RT   at the G2/M transition.";
RL   J. Biol. Chem. 285:16978-16990(2010).
RN   [37]
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   [38]
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   [39]
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.,
RA   Vervoorts J., 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   [40]
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.,
RA   Buerckstuemmer T., 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   [41]
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   [42]
RP   FUNCTION AS CTNNB1 KINASE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   PTPN6 AND CTNNB1.
RX   PubMed=21262353; DOI=10.1016/j.cellsig.2011.01.019;
RA   Fiset A., Xu E., Bergeron S., Marette A., Pelletier G.,
RA   Siminovitch K.A., 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   [43]
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   [44]
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   [45]
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
RT   damage response in human embryonic stem cells.";
RL   Stem Cells 29:651-659(2011).
RN   [46]
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   [47]
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   [48]
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   [49]
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   [50]
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   [51]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [52]
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   [53]
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.,
RA   Massague J., Pavletich N.P.;
RT   "Mechanism of CDK activation revealed by the structure of a cyclinA-
RT   CDK2 complex.";
RL   Nature 376:313-320(1995).
RN   [54]
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
RT   complex with cell cycle-regulatory protein CksHs1.";
RL   Cell 84:863-874(1996).
RN   [55]
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
RT   with and without ATP: bound waters and natural ligand as guides for
RT   inhibitor design.";
RL   J. Med. Chem. 39:4540-4546(1996).
RN   [56]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CG2A AND KIP1.
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
RT   bound to the cyclin A-Cdk2 complex.";
RL   Nature 382:325-331(1996).
RN   [57]
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   [58]
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
RT   of human CDK2, a cell cycle kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:2735-2740(1996).
RN   [59]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH STAUROSPORINE,
RP   AND ENZYME 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   [60]
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.,
RA   Kim S.H., Lockhart D.J., Schultz P.G.;
RT   "Exploiting chemical libraries, structure, and genomics in the search
RT   for kinase inhibitors.";
RL   Science 281:533-538(1998).
RN   [61]
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
RT   structure-guided design and SAR.";
RL   Bioorg. Med. Chem. Lett. 16:1353-1357(2006).
RN   [62]
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.,
RA   Dokurno P., Howes R., Borgognoni J., Drysdale M.J., Finch H.,
RA   Hubbard R.E., Jackson P.S., Kierstan P., Lentzen G., Moore J.D.,
RA   Murray J.B., 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   [63]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-288 IN COMPLEX WITH CCNB1,
RP   AND FUNCTION.
RX   PubMed=17495531;
RA   Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R.,
RA   Johnson L.N.;
RT   "Cyclin B and cyclin A confer different substrate recognition
RT   properties on CDK2.";
RL   Cell Cycle 6:1350-1359(2007).
RN   [64]
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.,
RA   Willis A., Noble M.E.M., Endicott J.A.;
RT   "How tyrosine 15 phosphorylation inhibits the activity of cyclin-
RT   dependent kinase 2-cyclin A.";
RL   J. Biol. Chem. 282:3173-3181(2007).
RN   [65]
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   [66]
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.,
RA   Lewis E.J., McMenamin R.L., Navarro E.F., O'Brien M.A., O'Reilly M.,
RA   Reule M., Saxty G., Seavers L.C., Smith D.M., Squires M.S.,
RA   Trewartha G., 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
RT   inhibitor using fragment-based X-ray crystallography and structure
RT   based drug design.";
RL   J. Med. Chem. 51:4986-4999(2008).
RN   [67]
RP   X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-296 IN COMPLEX WITH ATP
RP   AND MAGNESIUM, 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   [68]
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.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in the control
CC       of the cell cycle; essential for meiosis, but dispensable for
CC       mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1,
CC       BRCA2, MYC, NPAT, EZH2. Interacts with cyclins A, B1, B3, D, or E.
CC       Triggers duplication of centrosomes and DNA. Acts at the G1-S
CC       transition to promote the E2F transcriptional program and the
CC       initiation of DNA synthesis, and modulates G2 progression;
CC       controls the timing of entry into mitosis/meiosis by controlling
CC       the subsequent activation of cyclin B/CDK1 by phosphorylation, and
CC       coordinates the activation of cyclin B/CDK1 at the centrosome and
CC       in the nucleus. Crucial role in orchestrating a fine balance
CC       between cellular proliferation, cell death, and DNA repair in
CC       human embryonic stem cells (hESCs). Activity of CDK2 is maximal
CC       during S phase and G2; activated by interaction with cyclin E
CC       during the early stages of DNA synthesis to permit G1-S
CC       transition, and subsequently activated by cyclin A2 (cyclin A1 in
CC       germ cells) during the late stages of DNA replication to drive the
CC       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
CC       that prevents cells with damaged DNA from initiating mitosis;
CC       regulates homologous recombination-dependent repair by
CC       phosphorylating BRCA2, this phosphorylation is low in S phase when
CC       recombination is active, but increases as cells progress towards
CC       mitosis. In response to DNA damage, double-strand break repair by
CC       homologous recombination a reduction of CDK2-mediated BRCA2
CC       phosphorylation. Phosphorylation of RB1 disturbs its interaction
CC       with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its
CC       dissociates from unduplicated centrosomes, thus initiating
CC       centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of
CC       NPAT at G1-S transition and until prophase stimulates the NPAT-
CC       mediated activation of histone gene transcription during S phase.
CC       Required for vitamin D-mediated growth inhibition by being itself
CC       inactivated. Involved in the nitric oxide- (NO) mediated signaling
CC       in a nitrosylation/activation-dependent manner. USP37 is activated
CC       by phosphorylation and thus triggers G1-S transition. CTNNB1
CC       phosphorylation regulates insulin internalization. {ECO:0000250,
CC       ECO:0000269|PubMed:10499802, ECO:0000269|PubMed:10884347,
CC       ECO:0000269|PubMed:10995386, ECO:0000269|PubMed:10995387,
CC       ECO:0000269|PubMed:11051553, ECO:0000269|PubMed:11113184,
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}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Phosphorylation at Thr-14 or Tyr-15 inactivates
CC       the enzyme, while phosphorylation at Thr-160 activates it.
CC       Inhibited by 1,25-dihydroxyvitamin D(3) (1,25-(OH)(2)D(3)), AG-
CC       024322, N-(4-Piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-
CC       pyrazole-3-carboxamide (AT7519), R547 (Ro-4584820), purine,
CC       pyrimidine and pyridine derivatives, 2-aminopyrimidines,
CC       paullones, thiazo derivatives, macrocyclic quinoxalin-2-one,
CC       pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine, 2-(1-
CC       ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine
CC       (roscovitine, seliciclib and CYC202), SNS-032 (BMS-387032),
CC       triazolo[1,5-a]pyrimidines, staurosporine and olomoucine.
CC       Stimulated by MYC. Inactivated by CDKN1A (p21).
CC       {ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:9030781,
CC       ECO:0000269|PubMed:9334743}.
CC   -!- SUBUNIT: Found in a complex with CABLES1, CCNA1 and CCNE1.
CC       Interacts with CABLES1 (By similarity). Interacts with UHRF2. Part
CC       of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with
CC       the Speedy/Ringo proteins SPDYA and SPDYC. Found in a complex with
CC       both SPDYA and CDKN1B/KIP1. Binds to RB1 and CDK7. Binding to
CC       CDKN1A (p21) leads to CDK2/cyclin E inactivation at the G1-S phase
CC       DNA damage checkpoint, thereby arresting cells at the G1-S
CC       transition during DNA repair. Associated with PTPN6 and beta-
CC       catenin/CTNNB1. Interacts with CACUL1. May interact with CEP63.
CC       {ECO:0000250, ECO:0000269|PubMed:10499802,
CC       ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:11980914,
CC       ECO:0000269|PubMed:12185076, ECO:0000269|PubMed:12839962,
CC       ECO:0000269|PubMed:12972555, 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:7630397,
CC       ECO:0000269|PubMed:8610110, ECO:0000269|PubMed:8684460,
CC       ECO:0000269|PubMed:8756328, ECO:0000269|PubMed:9334743}.
CC   -!- INTERACTION:
CC       P20248:CCNA2; NbExp=19; IntAct=EBI-375096, EBI-457097;
CC       O95067:CCNB2; NbExp=2; IntAct=EBI-375096, EBI-375024;
CC       P24864:CCNE1; NbExp=10; IntAct=EBI-375096, EBI-519526;
CC       O96020:CCNE2; NbExp=7; IntAct=EBI-375096, EBI-375033;
CC       P51946:CCNH; NbExp=2; IntAct=EBI-375096, EBI-741406;
CC       P38936:CDKN1A; NbExp=14; IntAct=EBI-375096, EBI-375077;
CC       P46527:CDKN1B; NbExp=16; IntAct=EBI-375096, EBI-519280;
CC       Q16667:CDKN3; NbExp=3; IntAct=EBI-375096, EBI-1031527;
CC       P61024:CKS1B; NbExp=3; IntAct=EBI-375096, EBI-456371;
CC       Q09472:EP300; NbExp=5; IntAct=EBI-375096, EBI-447295;
CC       Q969H0-4:FBXW7; NbExp=2; IntAct=EBI-375096, EBI-6502391;
CC       Q08619:Ifi205b (xeno); NbExp=2; IntAct=EBI-375096, EBI-8064290;
CC       Q9Y6K9:IKBKG; NbExp=4; IntAct=EBI-375096, EBI-81279;
CC       P06400:RB1; NbExp=3; IntAct=EBI-375096, EBI-491274;
CC       Q9UBI4:STOML1; NbExp=2; IntAct=EBI-375096, EBI-2681162;
CC       Q96PU4:UHRF2; NbExp=5; IntAct=EBI-375096, EBI-625304;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome. Nucleus, Cajal body. Cytoplasm.
CC       Endosome. Note=Localized at the centrosomes in late G2 phase after
CC       separation of the centrosomes but before the start of prophase.
CC       Nuclear-cytoplasmic trafficking is mediated during the inhibition
CC       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
CC       TGFB1-mediated apoptosis.
CC   -!- PTM: Phosphorylated at Thr-160 by CDK7 in a CAK complex.
CC       Phosphorylation at Thr-160 promotes kinase activity, whereas
CC       phosphorylation at Tyr-15 by WEE1 reduces slightly kinase
CC       activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2
CC       phases before being dephosphorylated by CDC25A.
CC       {ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:1396589,
CC       ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401,
CC       ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17373709,
CC       ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:19369195,
CC       ECO:0000269|PubMed:19690332, ECO:0000269|PubMed:20147522,
CC       ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702}.
CC   -!- PTM: Nitrosylated after treatment with nitric oxide (DETA-NO).
CC       {ECO:0000269|PubMed:20079829}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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   UniGene; Hs.19192; -.
DR   UniGene; Hs.689624; -.
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; 2HIC; Model; -; A=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; 4CFN; X-ray; 2.20 A; A/C=1-298.
DR   PDB; 4CFW; X-ray; 2.45 A; A/C=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   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; 2HIC; -.
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; 4CFN; -.
DR   PDBsum; 4CFW; -.
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   ProteinModelPortal; P24941; -.
DR   SMR; P24941; 1-298.
DR   BioGrid; 107452; 575.
DR   DIP; DIP-161N; -.
DR   IntAct; P24941; 67.
DR   MINT; MINT-96328; -.
DR   STRING; 9606.ENSP00000266970; -.
DR   BindingDB; P24941; -.
DR   ChEMBL; CHEMBL3038470; -.
DR   DrugBank; DB06616; Bosutinib.
DR   GuidetoPHARMACOLOGY; 1973; -.
DR   PhosphoSite; P24941; -.
DR   DMDM; 116051; -.
DR   MaxQB; P24941; -.
DR   PaxDb; P24941; -.
DR   PRIDE; P24941; -.
DR   DNASU; 1017; -.
DR   Ensembl; ENST00000266970; ENSP00000266970; ENSG00000123374. [P24941-1]
DR   Ensembl; ENST00000354056; ENSP00000243067; ENSG00000123374. [P24941-2]
DR   GeneID; 1017; -.
DR   KEGG; hsa:1017; -.
DR   UCSC; uc001sit.4; human. [P24941-1]
DR   UCSC; uc001siu.4; human. [P24941-2]
DR   CTD; 1017; -.
DR   GeneCards; GC12P056360; -.
DR   HGNC; HGNC:1771; CDK2.
DR   HPA; CAB013115; -.
DR   MIM; 116953; gene.
DR   neXtProt; NX_P24941; -.
DR   PharmGKB; PA101; -.
DR   eggNOG; COG0515; -.
DR   GeneTree; ENSGT00760000119154; -.
DR   HOGENOM; HOG000233024; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; P24941; -.
DR   KO; K02206; -.
DR   OrthoDB; EOG7966H8; -.
DR   PhylomeDB; P24941; -.
DR   TreeFam; TF101021; -.
DR   BRENDA; 2.7.11.22; 2681.
DR   Reactome; REACT_1095; Activation of the pre-replicative complex.
DR   Reactome; REACT_111214; G0 and Early G1.
DR   Reactome; REACT_1156; Orc1 removal from chromatin.
DR   Reactome; REACT_1221; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; REACT_1625; p53-Dependent G1 DNA Damage Response.
DR   Reactome; REACT_169168; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; REACT_169185; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; REACT_1857; Cyclin A/B1 associated events during G2/M transition.
DR   Reactome; REACT_1915; G2 Phase.
DR   Reactome; REACT_24970; Factors involved in megakaryocyte development and platelet production.
DR   Reactome; REACT_27271; Meiotic recombination.
DR   Reactome; REACT_308; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR   Reactome; REACT_6769; Activation of ATR in response to replication stress.
DR   Reactome; REACT_6837; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; REACT_9003; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; REACT_9029; Cyclin A:Cdk2-associated events at S phase entry.
DR   SignaLink; P24941; -.
DR   ChiTaRS; CDK2; human.
DR   EvolutionaryTrace; P24941; -.
DR   GeneWiki; Cyclin-dependent_kinase_2; -.
DR   GenomeRNAi; 1017; -.
DR   NextBio; 4273; -.
DR   PRO; PR:P24941; -.
DR   Bgee; P24941; -.
DR   CleanEx; HS_CDK2; -.
DR   ExpressionAtlas; P24941; baseline and differential.
DR   Genevestigator; P24941; -.
DR   GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; TAS:UniProtKB.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0000793; C:condensed chromosome; 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:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription factor 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:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0071732; P:cellular response to nitric oxide; TAS:UniProtKB.
DR   GO; GO:0051298; P:centrosome duplication; TAS:UniProtKB.
DR   GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
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; TAS:Reactome.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:UniProtKB.
DR   GO; GO:0016572; P:histone phosphorylation; IDA:GOC.
DR   GO; GO:0007126; P:meiotic nuclear division; TAS:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; TAS:UniProtKB.
DR   GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR   GO; GO:0032298; P:positive regulation of DNA-dependent DNA replication initiation; IEA:Ensembl.
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:0007265; P:Ras protein signal transduction; IEP:BHF-UCL.
DR   GO; GO:0060968; P:regulation of gene silencing; IDA:UniProtKB.
DR   GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR002290; Ser/Thr_dual-sp_kinase.
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;
KW   Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
KW   DNA damage; DNA repair; Endosome; Kinase; Magnesium; Meiosis;
KW   Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; S-nitrosylation;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    298       Cyclin-dependent kinase 2.
FT                                /FTId=PRO_0000085769.
FT   DOMAIN        4    286       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      10     18       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:17095507,
FT                                ECO:0000269|PubMed:21565702}.
FT   NP_BIND      81     83       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:17095507,
FT                                ECO:0000269|PubMed:21565702}.
FT   NP_BIND     129    132       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:17095507,
FT                                ECO:0000269|PubMed:21565702}.
FT   ACT_SITE    127    127       Proton acceptor.
FT   METAL       132    132       Magnesium; catalytic.
FT                                {ECO:0000269|PubMed:21565702}.
FT   METAL       145    145       Magnesium; catalytic.
FT                                {ECO:0000269|PubMed:21565702}.
FT   BINDING      33     33       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:17095507,
FT                                ECO:0000269|PubMed:21565702}.
FT   BINDING      86     86       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:17095507,
FT                                ECO:0000269|PubMed:21565702}.
FT   BINDING     145    145       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:17095507,
FT                                ECO:0000269|PubMed:21565702}.
FT   SITE          9      9       CDK7 binding.
FT   SITE         88     89       CDK7 binding.
FT   SITE        166    166       CDK7 binding.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000269|PubMed:19608861,
FT                                ECO:0000269|PubMed:22814378}.
FT   MOD_RES       6      6       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19608861}.
FT   MOD_RES      14     14       Phosphothreonine.
FT                                {ECO:0000269|PubMed:1396589,
FT                                ECO:0000269|PubMed:17095507}.
FT   MOD_RES      15     15       Phosphotyrosine; by WEE1.
FT                                {ECO:0000269|PubMed:1396589,
FT                                ECO:0000269|PubMed:17095507,
FT                                ECO:0000269|PubMed:19690332}.
FT   MOD_RES      19     19       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:19369195}.
FT   MOD_RES     160    160       Phosphothreonine; by CAK and CCRK.
FT                                {ECO:0000269|PubMed:1396589,
FT                                ECO:0000269|PubMed:14597612,
FT                                ECO:0000269|PubMed:16325401,
FT                                ECO:0000269|PubMed:17095507,
FT                                ECO:0000269|PubMed:17570665,
FT                                ECO:0000269|PubMed:20147522,
FT                                ECO:0000269|PubMed:20360007,
FT                                ECO:0000269|PubMed:21565702}.
FT   VAR_SEQ     163    196       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_041998.
FT   VARIANT      15     15       Y -> S (in dbSNP:rs3087335).
FT                                /FTId=VAR_016157.
FT   VARIANT      18     18       V -> L (in dbSNP:rs11554376).
FT                                /FTId=VAR_053927.
FT   VARIANT      45     45       P -> L (in a glioblastoma multiforme
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041972.
FT   VARIANT     290    290       T -> S (in dbSNP:rs2069413).
FT                                {ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|Ref.6}.
FT                                /FTId=VAR_019988.
FT   MUTAGEN       9      9       K->F: Reduced phosphorylation by CAK.
FT                                {ECO:0000269|PubMed:17373709}.
FT   MUTAGEN      14     14       T->A: 2-fold increase in activity.
FT                                {ECO:0000269|PubMed:1396589}.
FT   MUTAGEN      15     15       Y->F: 2-fold increase in activity.
FT                                {ECO:0000269|PubMed:1396589}.
FT   MUTAGEN      88     89       KK->EV: Reduced phosphorylation by CAK.
FT                                {ECO:0000269|PubMed:17373709}.
FT   MUTAGEN     160    160       T->A: Abolishes activity.
FT                                {ECO:0000269|PubMed:1396589}.
FT   MUTAGEN     166    166       L->R: Reduced phosphorylation by CAK and
FT                                reduced kinase activity.
FT                                {ECO:0000269|PubMed:17373709}.
FT   CONFLICT      8     12       EKIGE -> AQIGQ (in Ref. 5; BAA32794).
FT                                {ECO:0000305}.
FT   CONFLICT     25     29       LTGEV -> STGQM (in Ref. 5; BAA32794).
FT                                {ECO:0000305}.
FT   CONFLICT    272    277       NKRISA -> YKRFST (in Ref. 5; BAA32794).
FT                                {ECO:0000305}.
FT   CONFLICT    286    287       FQ -> LE (in Ref. 5; BAA32794).
FT                                {ECO:0000305}.
FT   HELIX         1      3
FT   STRAND        4     12
FT   STRAND       14     23
FT   TURN         24     26
FT   STRAND       29     35
FT   STRAND       39     41
FT   STRAND       42     44
FT   HELIX        46     54
FT   HELIX        55     57
FT   STRAND       66     72
FT   STRAND       75     81
FT   STRAND       84     86
FT   HELIX        87     93
FT   TURN         94     97
FT   HELIX       101    120
FT   HELIX       130    132
FT   STRAND      133    135
FT   TURN        137    139
FT   STRAND      141    143
FT   HELIX       148    152
FT   HELIX       156    158
FT   STRAND      159    161
FT   HELIX       162    168
FT   HELIX       171    174
FT   STRAND      178    180
FT   HELIX       183    198
FT   HELIX       208    219
FT   TURN        224    226
FT   HELIX       230    232
FT   HELIX       248    251
FT   STRAND      252    254
FT   HELIX       257    266
FT   TURN        271    273
FT   HELIX       277    281
FT   HELIX       284    286
FT   TURN        287    289
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
//
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