[1]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6385987 [NCBI, ExPASy, EBI, Israel, Japan]
Wawrzynczak E.J.,
Perham R.N.;
"Isolation and nucleotide sequence of a cDNA encoding human calmodulin.";
Biochem. Int. 9:177-185(1984).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2445749 [NCBI, ExPASy, EBI, Israel, Japan]
Sengupta B.,
Friedberg F.,
Detera-Wadleigh S.D.;
"Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species.";
J. Biol. Chem. 262:16663-16670(1987).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3182832 [NCBI, ExPASy, EBI, Israel, Japan]
Fischer R.,
Koller M.,
Flura M.,
Mathews S.,
Strehler-Page M.A.,
Krebs J.,
Penniston J.T.,
Carafoli E.,
Strehler E.E.;
"Multiple divergent mRNAs code for a single human calmodulin.";
J. Biol. Chem. 263:17055-17062(1988).
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM3).
TISSUE=Blood;
DOI=10.1016/0167-4781(90)90203-E; PubMed=2223880 [NCBI, ExPASy, EBI, Israel, Japan]
Koller M.,
Schnyder B.,
Strehler E.E.;
"Structural organization of the human CaMIII calmodulin gene.";
Biochim. Biophys. Acta 1087:180-189(1990).
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM1).
TISSUE=Blood;
PubMed=7925473 [NCBI, ExPASy, EBI, Israel, Japan]
Rhyner J.A.,
Ottiger M.,
Wicki R.,
Greenwood T.M.,
Strehler E.E.;
"Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2.";
Eur. J. Biochem. 225:71-82(1994).
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[6]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphoma;
Kato S.;
"Human calmodulin cDNA.";
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
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[7]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CALM2).
DOI=10.1016/S0143-4160(98)90028-8; PubMed=9681195 [NCBI, ExPASy, EBI, Israel, Japan]
Toutenhoofd S.L.,
Foletti D.,
Wicki R.,
Rhyner J.A.,
Garcia F.,
Tolon R.,
Strehler E.E.;
"Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3.";
Cell Calcium 23:323-338(1998).
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[8]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM1; CALM2 AND CALM3).
Kalnine N.,
Chen X.,
Rolfs A.,
Halleck A.,
Hines L.,
Eisenstein S.,
Koundinya M.,
Raphael J.,
Moreira D.,
Kelley T.,
LaBaer J.,
Lin Y.,
Phelan M.,
Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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[9]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM2).
Halleck A.,
Ebert L.,
Mkoundinya M.,
Schick M.,
Eisenstein S.,
Neubert P.,
Kstrang K.,
Schatten R.,
Shen B.,
Henze S.,
Mar W.,
Korn B.,
Zuo D.,
Hu Y.,
LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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[10]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CALM1).
DOI=10.1038/nature01348; PubMed=12508121 [NCBI, ExPASy, EBI, Israel, Japan]
Heilig R.,
Eckenberg R.,
Petit J.-L.,
Fonknechten N.,
Da Silva C.,
Cattolico L.,
Levy M.,
Barbe V.,
De Berardinis V.,
Ureta-Vidal A.,
Pelletier E.,
Vico V.,
Anthouard V.,
Rowen L.,
Madan A.,
Qin S.,
Sun H.,
Du H.,
Pepin K., ![]()
Artiguenave F.,
Robert C.,
Cruaud C.,
Bruels T.,
Jaillon O.,
Friedlander L.,
Samson G.,
Brottier P.,
Cure S.,
Segurens B.,
Aniere F.,
Samain S.,
Crespeau H.,
Abbasi N.,
Aiach N.,
Boscus D.,
Dickhoff R.,
Dors M.,
Dubois I.,
Friedman C.,
Gouyvenoux M.,
James R.,
Madan A.,
Mairey-Estrada B.,
Mangenot S.,
Martins N.,
Menard M.,
Oztas S.,
Ratcliffe A.,
Shaffer T.,
Trask B.,
Vacherie B.,
Bellemere C.,
Belser C.,
Besnard-Gonnet M.,
Bartol-Mavel D.,
Boutard M.,
Briez-Silla S.,
Combette S.,
Dufosse-Laurent V.,
Ferron C.,
Lechaplais C.,
Louesse C.,
Muselet D.,
Magdelenat G.,
Pateau E.,
Petit E.,
Sirvain-Trukniewicz P.,
Trybou A.,
Vega-Czarny N.,
Bataille E.,
Bluet E.,
Bordelais I.,
Dubois M.,
Dumont C.,
Guerin T.,
Haffray S.,
Hammadi R.,
Muanga J.,
Pellouin V.,
Robert D.,
Wunderle E.,
Gauguet G.,
Roy A.,
Sainte-Marthe L.,
Verdier J.,
Verdier-Discala C.,
Hillier L.W.,
Fulton L.,
McPherson J.,
Matsuda F.,
Wilson R.,
Scarpelli C.,
Gyapay G.,
Wincker P.,
Saurin W.,
Quetier F.,
Waterston R.,
Hood L.,
Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
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[11]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CALM2).
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W.,
Graves T.A.,
Fulton R.S.,
Fulton L.A.,
Pepin K.H.,
Minx P.,
Wagner-McPherson C.,
Layman D.,
Wylie K.,
Sekhon M.,
Becker M.C.,
Fewell G.A.,
Delehaunty K.D.,
Miner T.L.,
Nash W.E.,
Kremitzki C.,
Oddy L.,
Du H.,
Sun H., ![]()
Bradshaw-Cordum H.,
Ali J.,
Carter J.,
Cordes M.,
Harris A.,
Isak A.,
van Brunt A.,
Nguyen C.,
Du F.,
Courtney L.,
Kalicki J.,
Ozersky P.,
Abbott S.,
Armstrong J.,
Belter E.A.,
Caruso L.,
Cedroni M.,
Cotton M.,
Davidson T.,
Desai A.,
Elliott G.,
Erb T.,
Fronick C.,
Gaige T.,
Haakenson W.,
Haglund K.,
Holmes A.,
Harkins R.,
Kim K.,
Kruchowski S.S.,
Strong C.M.,
Grewal N.,
Goyea E.,
Hou S.,
Levy A.,
Martinka S.,
Mead K.,
McLellan M.D.,
Meyer R.,
Randall-Maher J.,
Tomlinson C.,
Dauphin-Kohlberg S.,
Kozlowicz-Reilly A.,
Shah N.,
Swearengen-Shahid S.,
Snider J.,
Strong J.T.,
Thompson J.,
Yoakum M.,
Leonard S.,
Pearman C.,
Trani L.,
Radionenko M.,
Waligorski J.E.,
Wang C.,
Rock S.M.,
Tin-Wollam A.-M.,
Maupin R.,
Latreille P.,
Wendl M.C.,
Yang S.-P.,
Pohl C.,
Wallis J.W.,
Spieth J.,
Bieri T.A.,
Berkowicz N.,
Nelson J.O.,
Osborne J.,
Ding L.,
Meyer R.,
Sabo A.,
Shotland Y.,
Sinha P.,
Wohldmann P.E.,
Cook L.L.,
Hickenbotham M.T.,
Eldred J.,
Williams D.,
Jones T.A.,
She X.,
Ciccarelli F.D.,
Izaurralde E.,
Taylor J.,
Schmutz J.,
Myers R.M.,
Cox D.R.,
Huang X.,
McPherson J.D.,
Mardis E.R.,
Clifton S.W.,
Warren W.C.,
Chinwalla A.T.,
Eddy S.R.,
Marra M.A.,
Ovcharenko I.,
Furey T.S.,
Miller W.,
Eichler E.E.,
Bork P.,
Suyama M.,
Torrents D.,
Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
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[12]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CALM1; CALM2 AND CALM3).
TISSUE=Brain, Lung, Lymph, Placenta, and Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[13]
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PROTEIN SEQUENCE OF 2-149, ACETYLATION AT ALA-2, AND METHYLATION AT LYS-116.
TISSUE=Brain;
DOI=10.1021/bi00539a041; PubMed=7093203 [NCBI, ExPASy, EBI, Israel, Japan]
Sasagawa T.,
Ericsson L.H.,
Walsh K.A.,
Schreiber W.E.,
Fischer E.H.,
Titani K.;
"Complete amino acid sequence of human brain calmodulin.";
Biochemistry 21:2565-2569(1982).
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[14]
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PROTEIN SEQUENCE OF 2-31 AND 92-107, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V.,
Bensaad K.,
Vousden K.H.;
Submitted (FEB-2008) to UniProtKB.
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[15]
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PROTEIN SEQUENCE OF 92-107, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G.,
Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
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[16]
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INTERACTION WITH TTN.
DOI=10.1038/27603; PubMed=9804419 [NCBI, ExPASy, EBI, Israel, Japan]
Mayans O.,
van der Ven P.F.M.,
Wilm M.,
Mues A.,
Young P.,
Furst D.O.,
Wilmanns M.,
Gautel M.;
"Structural basis for activation of the titin kinase domain during myofibrillogenesis.";
Nature 395:863-869(1998).
|
[17]
|
INTERACTION WITH SRY.
PubMed=12871148 [NCBI, ExPASy, EBI, Israel, Japan]
Kelly S.,
Yotis J.,
Macris M.,
Harley V.;
"Recombinant expression, purification and characterisation of the HMG domain of human SRY.";
Protein Pept. Lett. 10:281-286(2003).
|
[18]
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INTERACTION WITH SRY.
DOI=10.1210/me.2004-0334; PubMed=15746192 [NCBI, ExPASy, EBI, Israel, Japan]
Sim H.,
Rimmer K.,
Kelly S.,
Ludbrook L.M.,
Clayton A.H.,
Harley V.R.;
"Defective calmodulin-mediated nuclear transport of the sex-determining region of the Y chromosome (SRY) in XY sex reversal.";
Mol. Endocrinol. 19:1884-1892(2005).
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[19]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J.,
Moritz A.,
Lee K.A.,
Guo A.,
Goss V.L.,
Spek E.J.,
Zhang H.,
Zha X.-M.,
Polakiewicz R.D.,
Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
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[20]
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FUNCTION, INTERACTION WITH CEP110, AND SUBCELLULAR LOCATION.
DOI=10.1091/mbc.E06-04-0371; PubMed=16760425 [NCBI, ExPASy, EBI, Israel, Japan]
Tsang W.Y.,
Spektor A.,
Luciano D.J.,
Indjeian V.B.,
Chen Z.,
Salisbury J.L.,
Sanchez I.,
Dynlacht B.D.;
"CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability.";
Mol. Biol. Cell 17:3423-3434(2006).
|
[21]
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INTERACTION WITH CEP97 AND CEP110.
DOI=10.1016/j.cell.2007.06.027; PubMed=17719545 [NCBI, ExPASy, EBI, Israel, Japan]
Spektor A.,
Tsang W.Y.,
Khoo D.,
Dynlacht B.D.;
"Cep97 and CP110 suppress a cilia assembly program.";
Cell 130:678-690(2007).
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[22]
|
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H.,
Horn D.M.,
Tang N.,
Mathivanan S.,
Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
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[23]
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STRUCTURE BY NMR OF 95-104.
DOI=10.1073/pnas.96.3.903; PubMed=9927666 [NCBI, ExPASy, EBI, Israel, Japan]
Siedlecka M.,
Goch G.,
Ejchart A.,
Sticht H.,
Bierzyski A.;
"Alpha-helix nucleation by a calcium-binding peptide loop.";
Proc. Natl. Acad. Sci. U.S.A. 96:903-908(1999).
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[24]
|
STRUCTURE BY NMR OF 1-77 AND 83-149.
DOI=10.1038/nsb1101-990; PubMed=11685248 [NCBI, ExPASy, EBI, Israel, Japan]
Chou J.J.,
Li S.,
Klee C.B.,
Bax A.;
"Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains.";
Nat. Struct. Biol. 8:990-997(2001).
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[25]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
DOI=10.1016/0022-2836(92)90324-D; PubMed=1474585 [NCBI, ExPASy, EBI, Israel, Japan]
Chattopadhyaya R.,
Meador W.E.,
Means A.R.,
Quiocho F.A.;
"Calmodulin structure refined at 1.7 A resolution.";
J. Mol. Biol. 228:1177-1192(1992).
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[26]
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X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
DOI=10.1021/bi00255a006; PubMed=7803388 [NCBI, ExPASy, EBI, Israel, Japan]
Cook W.J.,
Walter L.J.,
Walter M.R.;
"Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex.";
Biochemistry 33:15259-15265(1994).
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[27]
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X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 6-149.
DOI=10.1038/415396a; PubMed=11807546 [NCBI, ExPASy, EBI, Israel, Japan]
Drum C.L.,
Yan S.-Z.,
Bard J.,
Shen Y.-Q.,
Lu D.,
Soelaiman S.,
Grabarek Z.,
Bohm A.,
Tang W.-J.;
"Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin.";
Nature 415:396-402(2002).
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[28]
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X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-149 IN COMPLEX WITH ANTHRAX EDEMA FACTOR CYA.
DOI=10.1093/emboj/cdf681; PubMed=12485993 [NCBI, ExPASy, EBI, Israel, Japan]
Shen Y.,
Lee Y.-S.,
Soelaiman S.,
Bergson P.,
Lu D.,
Chen A.,
Beckingham K.,
Grabarek Z.,
Mrksich M.,
Tang W.-J.;
"Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins.";
EMBO J. 21:6721-6732(2002).
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[29]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MARCKS.
DOI=10.1038/nsb900; PubMed=12577052 [NCBI, ExPASy, EBI, Israel, Japan]
Yamauchi E.,
Nakatsu T.,
Matsubara M.,
Kato H.,
Taniguchi H.;
"Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin.";
Nat. Struct. Biol. 10:226-231(2003).
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[30]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-150 IN COMPLEX WITH CACNA1C.
DOI=10.1038/nsmb1027; PubMed=16299511 [NCBI, ExPASy, EBI, Israel, Japan]
Van Petegem F.,
Chatelain F.C.,
Minor D.L. Jr.;
"Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex.";
Nat. Struct. Mol. Biol. 12:1108-1115(2005).
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[31]
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X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH ANTHRAX EDEMA FACTOR CYA.
DOI=10.1038/sj.emboj.7600574; PubMed=15719022 [NCBI, ExPASy, EBI, Israel, Japan]
Shen Y.,
Zhukovskaya N.L.,
Guo Q.,
Florian J.,
Tang W.-J.;
"Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor.";
EMBO J. 24:929-941(2005).
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