Example 3-1 contains a sequence entry from SWISS-PROT. This entry contains terms from the SWISS-PROT Field Definitions and Feature Table types, discussed later in this chapter. Example 3-1. Sample SWISS-PROT sequence entryID CDK2_HUMAN STANDARD; PRT; 298 AA. AC P24941; DT 01-MAR-1992 (Rel. 21, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Cell division protein kinase 2 (EC 2.7.1.-) (p33 protein kinase). GN CDK2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91330891; 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 SEQUENCE FROM N.A. RX MEDLINE=91367262; PubMed=1653904; 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 SEQUENCE FROM N.A. RX MEDLINE=92020980; PubMed=1717994; 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 SEQUENCE FROM N.A. RC TISSUE=Placenta; RA Strausberg R.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP PHOSPHORYLATION SITES. RX MEDLINE=93010995; 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX MEDLINE=93288132; PubMed=8510751; RA de Bondt H.L., Rosenblatt J., Jancarik J., Jones H.D., RA Morgan D.O., Kim S.-H.; RT "Crystal structure of cyclin-dependent kinase 2."; RL Nature 363:595-602(1993). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CYCLIN A. RX MEDLINE=95356811; PubMed=7630397; 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 RT cyclinA-CDK2 complex."; RL Nature 376:313-320(1995). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF COMPLEX WITH L868276. RX MEDLINE=96181476; PubMed=8610110; RA de Azevedo W.F. Jr., Muleer-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 RT inhibitor of human CDK2, a cell cycle kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 93:2735-2740(1996). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH CG2A AND KIP1. RX MEDLINE=96300318; PubMed=8684460; 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 [10] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH CG2A. RX MEDLINE=96313126; PubMed=8756328; 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 [11] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=97075215; PubMed=8917641; RA Schulze-Gahmen U., de Bondt H.L., Kim S.-H.; RT "High-resolution crystal structures of human cyclin-dependent kinase RT 2 with and without ATP: bound waters and natural ligand as guides for RT inhibitor design."; RL J. Med. Chem. 39:4540-4546(1996). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=97475219; PubMed=9334743; 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 RT the molecular interaction with CDK2."; RL Nat. Struct. Biol. 4:796-801(1997). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITG CKS1. RX MEDLINE=96182647; PubMed=8601310; 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 [14] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS). RX MEDLINE=98342369; PubMed=9677190; 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). CC -!- FUNCTION: PROBABLY INVOLVED IN THE CONTROL OF THE CELL CYCLE. CC INTERACTS WITH CYCLINS A, D, OR E. ACTIVITY OF CDK2 IS MAXIMAL CC DURING S PHASE AND G2. CC -!- ENZYME REGULATION: PHOSPHORYLATION AT THR-14 OR TYR-15 INACTIVATES CC THE ENZYME, WHILE PHOSPHORYLATION AT THR-160 ACTIVATES IT. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CDC2/CDKX SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61622; CAA43807.1; -. DR EMBL; X62071; CAA43985.1; -. DR EMBL; M68520; AAA35667.1; -. DR EMBL; BC003065; AAH03065.1; -. DR PIR; A41227; A41227. DR PIR; S16520; S16520. DR PIR; S17873; S17873. DR PDB; 1FIN; 27-JAN-97. DR PDB; 1HCK; 07-DEC-96. DR PDB; 1HCL; 07-DEC-96. DR PDB; 1AQ1; 12-NOV-97. DR PDB; 1JST; 11-JAN-97. DR PDB; 1JSU; 29-JUL-97. DR PDB; 1BUH; 09-SEP-98. DR PDB; 1B38; 23-DEC-98. DR PDB; 1B39; 23-DEC-98. DR PDB; 1CKP; 13-JAN-99. DR Genew; HGNC:1771; CDK2. DR MIM; 116953; -. DR InterPro; IPR000719; Euk_pkinase. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; pkinase; 1. DR ProDom; PD000001; Euk_pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Cell cycle; Cell division; Mitosis; Phosphorylation; 3D-structure. FT DOMAIN 4 286 PROTEIN KINASE. FT NP_BIND 10 18 ATP (BY SIMILARITY). FT BINDING 33 33 ATP (BY SIMILARITY). FT ACT_SITE 127 127 BY SIMILARITY. FT MOD_RES 14 14 PHOSPHORYLATION. FT MOD_RES 15 15 PHOSPHORYLATION. FT MOD_RES 160 160 PHOSPHORYLATION (BY CAK). FT MUTAGEN 14 14 T->A: INCREASE ACTIVITY 2 FOLD. FT MUTAGEN 15 15 Y->F: INCREASE ACTIVITY 2 FOLD. FT MUTAGEN 160 160 T->A: ABOLISHES ACTIVITY. FT TURN 2 3 FT STRAND 4 12 FT STRAND 17 23 FT TURN 24 26 FT STRAND 29 35 FT HELIX 46 55 FT TURN 56 57 FT TURN 61 62 FT STRAND 63 63 FT STRAND 66 72 FT TURN 73 74 FT STRAND 75 81 FT STRAND 85 86 FT HELIX 87 93 FT TURN 94 97 FT HELIX 101 120 FT TURN 121 122 FT HELIX 130 132 FT STRAND 133 135 FT TURN 137 138 FT STRAND 141 143 FT TURN 146 147 FT HELIX 148 151 FT STRAND 157 157 FT TURN 159 160 FT STRAND 163 163 FT TURN 167 168 FT HELIX 171 174 FT TURN 175 176 FT TURN 182 182 FT HELIX 183 198 FT HELIX 208 219 FT TURN 224 226 FT TURN 228 229 FT HELIX 230 232 FT TURN 234 235 FT TURN 238 239 FT HELIX 248 251 FT TURN 253 254 FT HELIX 257 266 FT TURN 267 267 FT TURN 271 273 FT HELIX 277 280 FT TURN 281 282 FT HELIX 284 286 FT TURN 287 288 SQ SEQUENCE 298 AA; 33929 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 // |