Gene of rat Ca2+/calmodulin‐dependent protein kinase II α isoform — its cloning and whole structure
The gene encoding the α isoform of rat Ca2+/ calmodulin‐dependent protein kinase II was cloned, and its exon‐intron organization was analyzed. The coding region of cDNA consists of 18 exons spanning more than 50 kilobase pairs. Each of the discrete functional units, such as the ATP‐binding site, the...
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| Veröffentlicht in: | FEBS letters 1996-11, Vol.396 (2-3), p.333-336 |
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| container_end_page | 336 |
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| container_issue | 2-3 |
| container_start_page | 333 |
| container_title | FEBS letters |
| container_volume | 396 |
| creator | Nishioka, Nobuhiro Shiojiri, Masatoshi Kadota, Shiori Morinaga, Hisayo Kuwahara, Jun Arakawa, Toshiya Yamamoto, Shozo Yamauchi, Takashi |
| description | The gene encoding the α isoform of rat Ca2+/ calmodulin‐dependent protein kinase II was cloned, and its exon‐intron organization was analyzed. The coding region of cDNA consists of 18 exons spanning more than 50 kilobase pairs. Each of the discrete functional units, such as the ATP‐binding site, the autophosphorylation site responsible for Ca2+‐independent activity, the calmodulin‐binding site, and link structure is encoded by a single exon. The largest and smallest exons consist of 229 and 41 base pairs, respectively. All splice junction sequences flanking the introns conform to the consensus splice junction sequence and the GT‐AG splice rule. |
| doi_str_mv | 10.1016/0014-5793(96)01105-2 |
| format | Article |
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The coding region of cDNA consists of 18 exons spanning more than 50 kilobase pairs. Each of the discrete functional units, such as the ATP‐binding site, the autophosphorylation site responsible for Ca2+‐independent activity, the calmodulin‐binding site, and link structure is encoded by a single exon. The largest and smallest exons consist of 229 and 41 base pairs, respectively. 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The coding region of cDNA consists of 18 exons spanning more than 50 kilobase pairs. Each of the discrete functional units, such as the ATP‐binding site, the autophosphorylation site responsible for Ca2+‐independent activity, the calmodulin‐binding site, and link structure is encoded by a single exon. The largest and smallest exons consist of 229 and 41 base pairs, respectively. All splice junction sequences flanking the introns conform to the consensus splice junction sequence and the GT‐AG splice rule.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Base Composition</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Brain specific expression</subject><subject>Ca2+/calmodulin-dependent protein kinase II</subject><subject>Calcium-Calmodulin-Dependent Protein Kinase Type 2</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - genetics</subject><subject>CaM kinase II</subject><subject>Cloning, Molecular</subject><subject>Consensus Sequence</subject><subject>DNA, Complementary - genetics</subject><subject>Exons</subject><subject>Gene structure</subject><subject>Genomic Library</subject><subject>Introns</subject><subject>Isoenzymes - genetics</subject><subject>PCR</subject><subject>Phosphorylation</subject><subject>Polymerase Chain Reaction</subject><subject>Rats</subject><subject>Sequence Analysis, DNA</subject><subject>α Isoform</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1OwzAQhS0EKqVwA5C8QiAU6p_8eQlVWypVYgNry0km1OA4JU5UddcjsOAiXIRD9CQktKpmMZr5nkZvHkKXlNxTQsMhIdT3gkjwGxHeEkpJ4LEj1KdxxD3uh_Ex6h8kp-jMuXfSzjEVPdSLBQ1a1keLKVjAZY4rVeORYnfDVJmizBqj7XbzlcESbAa2xsuqrEFb_KGtcoBnM_z7g7Ur87Iq8HbzjXXtcGpKq-0bVjbDq0VpALu6atK6qeAcneTKOLjY9wF6nYxfRk_e_Hk6Gz3MvSUjlHmJUn7EVOIrFgIQ5vuKCwEBEUTxMCI8b1VJzEnavZWD4hn3BYg8CzPKY8IH6Hp3tzX82YCrZaFdCsYoC2XjZBQHrC3eCq_2wiYpIJPLSheqWst9NC2f7PhKG1gfMCWyS1920crOgxTt0KUvmZyMH1kHur0I_7eM_wHEHHtq</recordid><startdate>19961104</startdate><enddate>19961104</enddate><creator>Nishioka, Nobuhiro</creator><creator>Shiojiri, Masatoshi</creator><creator>Kadota, Shiori</creator><creator>Morinaga, Hisayo</creator><creator>Kuwahara, Jun</creator><creator>Arakawa, Toshiya</creator><creator>Yamamoto, Shozo</creator><creator>Yamauchi, Takashi</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19961104</creationdate><title>Gene of rat Ca2+/calmodulin‐dependent protein kinase II α isoform — its cloning and whole structure</title><author>Nishioka, Nobuhiro ; Shiojiri, Masatoshi ; Kadota, Shiori ; Morinaga, Hisayo ; Kuwahara, Jun ; Arakawa, Toshiya ; Yamamoto, Shozo ; Yamauchi, Takashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p2012-baa472ab4a26ee0244a399e5090a36703f012b830c5793fea3d349e9fd6d13803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Base Composition</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Brain specific expression</topic><topic>Ca2+/calmodulin-dependent protein kinase II</topic><topic>Calcium-Calmodulin-Dependent Protein Kinase Type 2</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - genetics</topic><topic>CaM kinase II</topic><topic>Cloning, Molecular</topic><topic>Consensus Sequence</topic><topic>DNA, Complementary - genetics</topic><topic>Exons</topic><topic>Gene structure</topic><topic>Genomic Library</topic><topic>Introns</topic><topic>Isoenzymes - genetics</topic><topic>PCR</topic><topic>Phosphorylation</topic><topic>Polymerase Chain Reaction</topic><topic>Rats</topic><topic>Sequence Analysis, DNA</topic><topic>α Isoform</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nishioka, Nobuhiro</creatorcontrib><creatorcontrib>Shiojiri, Masatoshi</creatorcontrib><creatorcontrib>Kadota, Shiori</creatorcontrib><creatorcontrib>Morinaga, Hisayo</creatorcontrib><creatorcontrib>Kuwahara, Jun</creatorcontrib><creatorcontrib>Arakawa, Toshiya</creatorcontrib><creatorcontrib>Yamamoto, Shozo</creatorcontrib><creatorcontrib>Yamauchi, Takashi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nishioka, Nobuhiro</au><au>Shiojiri, Masatoshi</au><au>Kadota, Shiori</au><au>Morinaga, Hisayo</au><au>Kuwahara, Jun</au><au>Arakawa, Toshiya</au><au>Yamamoto, Shozo</au><au>Yamauchi, Takashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gene of rat Ca2+/calmodulin‐dependent protein kinase II α isoform — its cloning and whole structure</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1996-11-04</date><risdate>1996</risdate><volume>396</volume><issue>2-3</issue><spage>333</spage><epage>336</epage><pages>333-336</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The gene encoding the α isoform of rat Ca2+/ calmodulin‐dependent protein kinase II was cloned, and its exon‐intron organization was analyzed. The coding region of cDNA consists of 18 exons spanning more than 50 kilobase pairs. Each of the discrete functional units, such as the ATP‐binding site, the autophosphorylation site responsible for Ca2+‐independent activity, the calmodulin‐binding site, and link structure is encoded by a single exon. The largest and smallest exons consist of 229 and 41 base pairs, respectively. All splice junction sequences flanking the introns conform to the consensus splice junction sequence and the GT‐AG splice rule.</abstract><cop>England</cop><pmid>8915014</pmid><doi>10.1016/0014-5793(96)01105-2</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1996-11, Vol.396 (2-3), p.333-336 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - metabolism Animals Base Composition Base Sequence Binding Sites Brain specific expression Ca2+/calmodulin-dependent protein kinase II Calcium-Calmodulin-Dependent Protein Kinase Type 2 Calcium-Calmodulin-Dependent Protein Kinases - genetics CaM kinase II Cloning, Molecular Consensus Sequence DNA, Complementary - genetics Exons Gene structure Genomic Library Introns Isoenzymes - genetics PCR Phosphorylation Polymerase Chain Reaction Rats Sequence Analysis, DNA α Isoform |
| title | Gene of rat Ca2+/calmodulin‐dependent protein kinase II α isoform — its cloning and whole structure |
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