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RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [10]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Brain, Lung, Lymph, Placenta, and Urinary bladder;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [11]
RP   STRUCTURE BY NMR OF 94-103.
RX   PubMed=9927666;
RA   Siedlecka M., Goch G., Ejchart A., Sticht H., Bierzyski A.;
RT   "Alpha-helix nucleation by a calcium-binding peptide loop.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:903-908(1999).
RN   [12]
RP   STRUCTURE BY NMR OF 1-76 AND 82-148.
RX   PubMed=11685248; DOI=10.1038/nsb1101-990;
RA   Chou J.J., Li S., Klee C.B., Bax A.;
RT   "Solution structure of Ca(2+)-calmodulin reveals flexible hand-like
RT   properties of its domains.";
RL   Nat. Struct. Biol. 8:990-997(2001).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=1474585;
RA   Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.;
RT   "Calmodulin structure refined at 1.7 A resolution.";
RL   J. Mol. Biol. 228:1177-1192(1992).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX   PubMed=7803388;
RA   Cook W.J., Walter L.J., Walter M.R.;
RT   "Drug binding by calmodulin: crystal structure of a calmodulin-
RT   trifluoperazine complex.";
RL   Biochemistry 33:15259-15265(1994).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 5-148.
RX   MEDLINE=21666515; PubMed=11807546; DOI=10.1038/415396a;
RA   Drum C.L., Yan S.-Z., Bard J., Shen Y.Q., Lu D., Soelaiman S.,
RA   Grabarek Z., Bohm A., Tang W.-J.;
RT   "Structural basis for the activation of anthrax adenylyl cyclase
RT   exotoxin by calmodulin.";
RL   Nature 415:396-402(2002).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-148.
RX   PubMed=12485993;
RA   Shen Y., Lee Y.-S., Soelaiman S., Bergson P., Lu D., Chen A.,
RA   Beckingham K., Grabarek Z., Mrksich M., Tang W.-J.;
RT   "Physiological calcium concentrations regulate calmodulin binding and
RT   catalysis of adenylyl cyclase exotoxins.";
RL   EMBO J. 21:6721-6732(2002).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=12577052; DOI=10.1038/nsb900;
RA   Yamauchi E., Nakatsu T., Matsubara M., Kato H., Taniguchi H.;
RT   "Crystal structure of a MARCKS peptide containing the calmodulin-
RT   binding domain in complex with Ca2+-calmodulin.";
RL   Nat. Struct. Biol. 10:226-231(2003).
CC   -!- FUNCTION: Calmodulin mediates the control of a large number of
CC       enzymes by Ca(2+). Among the enzymes to be stimulated by the
CC       calmodulin-Ca(2+) complex are a number of protein kinases and
CC       phosphatases.
CC   -!- PTM: Ubiquitylation results in a strongly decreased activity (By
CC       similarity).
CC   -!- PTM: Phosphorylation results in a decreased activity (By
CC       similarity).
CC   -!- MISCELLANEOUS: This protein has four functional calcium-binding
CC       sites.
CC   -!- SIMILARITY: Contains 4 EF-hand calcium-binding domains.
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; J04046; AAA51918.1; -.
DR   EMBL; M19311; AAA35641.1; -.
DR   EMBL; M27319; AAA35635.1; -.
DR   EMBL; U12022; AAB60644.1; -.
DR   EMBL; U11886; AAB60644.1; JOINED.
DR   EMBL; D45887; BAA08302.1; -.
DR   EMBL; U94728; AAC83174.1; -.
DR   EMBL; U94725; AAC83174.1; JOINED.
DR   EMBL; U94726; AAC83174.1; JOINED.
DR   EMBL; BT006818; AAP35464.1; -.
DR   EMBL; BT006855; AAP35501.1; -.
DR   EMBL; BT009916; AAP88918.1; -.
DR   EMBL; AC006536; AAD45181.1; -.
DR   EMBL; BC000454; AAH00454.1; -.



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