3.1 SWISS-PROT Example Flat File
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 entry
ID 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
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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
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