Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain
The SH2-B protein is an SH2-domain-containing molecule that interacts with a number of phosphorylated kinase and receptor molecules including the insulin receptor. Two isoforms of the SH2-B have been identified and have been proposed to arise through alternate splicing. Here we have identified a thi...
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| Veröffentlicht in: | Mammalian genome 1999-12, Vol.10 (12), p.1160-1167 |
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| creator | Nelms, Keats O'Neill, Thomas J Li, Shiqing Hubbard, Stevan R Gustafson, Thomas A Paul, William E |
| description | The SH2-B protein is an SH2-domain-containing molecule that interacts with a number of phosphorylated kinase and receptor molecules including the insulin receptor. Two isoforms of the SH2-B have been identified and have been proposed to arise through alternate splicing. Here we have identified a third isoform of the SH2-B protein, SH2-Bγ, that interacts specifically with the insulin receptor. This interaction required phosphorylation of residue Y1146 in the triple tyrosine motif within the activation loop of the IR kinase and is one of only two signaling molecules shown to interact directly with this residue of the insulin receptor kinase domain. The intron/exon structure of the SH2-B gene was determined. Alternate splice sites utilized to generate the different isoforms of the SH2-B protein were identified in the 3′ end of the SH2-B gene immediately downstream of the exon encoding the core of the SH2 domain. Additionally, the chromosomal location of the SH2-B gene was determined to be the distal arm of mouse Chromosome (Chr) 7 in a region linked to obesity in mice. |
| doi_str_mv | 10.1007/s003359901183 |
| format | Article |
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Two isoforms of the SH2-B have been identified and have been proposed to arise through alternate splicing. Here we have identified a third isoform of the SH2-B protein, SH2-Bγ, that interacts specifically with the insulin receptor. This interaction required phosphorylation of residue Y1146 in the triple tyrosine motif within the activation loop of the IR kinase and is one of only two signaling molecules shown to interact directly with this residue of the insulin receptor kinase domain. The intron/exon structure of the SH2-B gene was determined. Alternate splice sites utilized to generate the different isoforms of the SH2-B protein were identified in the 3′ end of the SH2-B gene immediately downstream of the exon encoding the core of the SH2 domain. Additionally, the chromosomal location of the SH2-B gene was determined to be the distal arm of mouse Chromosome (Chr) 7 in a region linked to obesity in mice.</description><identifier>ISSN: 0938-8990</identifier><identifier>EISSN: 1432-1777</identifier><identifier>DOI: 10.1007/s003359901183</identifier><identifier>PMID: 10594240</identifier><language>eng</language><publisher>United States: Springer-Verlag</publisher><subject>Adaptor Proteins, Signal Transducing ; alternative splicing ; Alternative Splicing - genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; chromosome 7 ; Chromosome Mapping ; chromosomes ; Cloning, Molecular ; exons ; Exons - genetics ; genes ; Insulin ; insulin receptors ; introns ; Introns - genetics ; Kinases ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Molecular Weight ; obesity ; Phosphorylation ; Phosphotyrosine - genetics ; Phosphotyrosine - metabolism ; Protein Binding ; Protein Isoforms - chemistry ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Proteins ; Receptor, Insulin - chemistry ; Receptor, Insulin - genetics ; Receptor, Insulin - metabolism ; RNA, Messenger - analysis ; RNA, Messenger - genetics ; SH2-B gene ; src Homology Domains - genetics ; Two-Hybrid System Techniques ; tyrosine</subject><ispartof>Mammalian genome, 1999-12, Vol.10 (12), p.1160-1167</ispartof><rights>Springer-Verlag New York Inc. 1999</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c477t-2381cd8d05a69ecabcc33d91edf07df2c6e8aab669e40b0156766aafa261cccd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10594240$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nelms, Keats</creatorcontrib><creatorcontrib>O'Neill, Thomas J</creatorcontrib><creatorcontrib>Li, Shiqing</creatorcontrib><creatorcontrib>Hubbard, Stevan R</creatorcontrib><creatorcontrib>Gustafson, Thomas A</creatorcontrib><creatorcontrib>Paul, William E</creatorcontrib><title>Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain</title><title>Mammalian genome</title><addtitle>Mamm Genome</addtitle><description>The SH2-B protein is an SH2-domain-containing molecule that interacts with a number of phosphorylated kinase and receptor molecules including the insulin receptor. Two isoforms of the SH2-B have been identified and have been proposed to arise through alternate splicing. Here we have identified a third isoform of the SH2-B protein, SH2-Bγ, that interacts specifically with the insulin receptor. This interaction required phosphorylation of residue Y1146 in the triple tyrosine motif within the activation loop of the IR kinase and is one of only two signaling molecules shown to interact directly with this residue of the insulin receptor kinase domain. The intron/exon structure of the SH2-B gene was determined. Alternate splice sites utilized to generate the different isoforms of the SH2-B protein were identified in the 3′ end of the SH2-B gene immediately downstream of the exon encoding the core of the SH2 domain. Additionally, the chromosomal location of the SH2-B gene was determined to be the distal arm of mouse Chromosome (Chr) 7 in a region linked to obesity in mice.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>alternative splicing</subject><subject>Alternative Splicing - genetics</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>chromosome 7</subject><subject>Chromosome Mapping</subject><subject>chromosomes</subject><subject>Cloning, Molecular</subject><subject>exons</subject><subject>Exons - genetics</subject><subject>genes</subject><subject>Insulin</subject><subject>insulin receptors</subject><subject>introns</subject><subject>Introns - genetics</subject><subject>Kinases</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>obesity</subject><subject>Phosphorylation</subject><subject>Phosphotyrosine - genetics</subject><subject>Phosphotyrosine - metabolism</subject><subject>Protein Binding</subject><subject>Protein Isoforms - chemistry</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Proteins</subject><subject>Receptor, Insulin - chemistry</subject><subject>Receptor, Insulin - genetics</subject><subject>Receptor, Insulin - metabolism</subject><subject>RNA, Messenger - analysis</subject><subject>RNA, Messenger - genetics</subject><subject>SH2-B gene</subject><subject>src Homology Domains - genetics</subject><subject>Two-Hybrid System Techniques</subject><subject>tyrosine</subject><issn>0938-8990</issn><issn>1432-1777</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0T1vFDEQBmALgcgRKGnBEhJVNoztXX-USQQEKRJFknrltWcPB5992LtI4ddjdCmAJtUU76ORZl5CXjM4ZQDqQwUQYjAGGNPiCdmwXvCOKaWekg0YoTvdsiPyotY7AKYkU8_JEYPB9LyHDXFnccGS7BJ-Iq37GFxI2xO6xYQ0Zmdj-NWynE6oTZ5OIfmW0zzT60vendMl0-Ub0pDqGkOiBR3ul1zo95BsRerzzob0kjybbaz46mEek9tPH28uLrurr5-_XJxdda5Xaum40Mx57WGw0qCzk3NCeMPQz6D8zJ1Ebe0kW9jDBGyQSkprZ8slc855cUzeH_buS_6xYl3GXagOY7QJ81pHacTQ90Y9CpnquQQNDb77D97ltX0rNgOcKSGY0U11B-VKrrXgPO5L2Nly39D4p6Txn5Kaf_OwdZ126P_Sh1YaeHsAs82j3ZZQx9tr3i5uDYJg2ojfgxqVMg</recordid><startdate>19991201</startdate><enddate>19991201</enddate><creator>Nelms, Keats</creator><creator>O'Neill, Thomas J</creator><creator>Li, Shiqing</creator><creator>Hubbard, Stevan R</creator><creator>Gustafson, Thomas A</creator><creator>Paul, William E</creator><general>Springer-Verlag</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19991201</creationdate><title>Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain</title><author>Nelms, Keats ; O'Neill, Thomas J ; Li, Shiqing ; Hubbard, Stevan R ; Gustafson, Thomas A ; Paul, William E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c477t-2381cd8d05a69ecabcc33d91edf07df2c6e8aab669e40b0156766aafa261cccd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>alternative splicing</topic><topic>Alternative Splicing - genetics</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>chromosome 7</topic><topic>Chromosome Mapping</topic><topic>chromosomes</topic><topic>Cloning, Molecular</topic><topic>exons</topic><topic>Exons - genetics</topic><topic>genes</topic><topic>Insulin</topic><topic>insulin receptors</topic><topic>introns</topic><topic>Introns - genetics</topic><topic>Kinases</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>obesity</topic><topic>Phosphorylation</topic><topic>Phosphotyrosine - genetics</topic><topic>Phosphotyrosine - metabolism</topic><topic>Protein Binding</topic><topic>Protein Isoforms - chemistry</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Proteins</topic><topic>Receptor, Insulin - chemistry</topic><topic>Receptor, Insulin - genetics</topic><topic>Receptor, Insulin - metabolism</topic><topic>RNA, Messenger - analysis</topic><topic>RNA, Messenger - genetics</topic><topic>SH2-B gene</topic><topic>src Homology Domains - genetics</topic><topic>Two-Hybrid System Techniques</topic><topic>tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nelms, Keats</creatorcontrib><creatorcontrib>O'Neill, Thomas J</creatorcontrib><creatorcontrib>Li, Shiqing</creatorcontrib><creatorcontrib>Hubbard, Stevan R</creatorcontrib><creatorcontrib>Gustafson, Thomas A</creatorcontrib><creatorcontrib>Paul, William E</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Mammalian genome</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nelms, Keats</au><au>O'Neill, Thomas J</au><au>Li, Shiqing</au><au>Hubbard, Stevan R</au><au>Gustafson, Thomas A</au><au>Paul, William E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain</atitle><jtitle>Mammalian genome</jtitle><addtitle>Mamm Genome</addtitle><date>1999-12-01</date><risdate>1999</risdate><volume>10</volume><issue>12</issue><spage>1160</spage><epage>1167</epage><pages>1160-1167</pages><issn>0938-8990</issn><eissn>1432-1777</eissn><abstract>The SH2-B protein is an SH2-domain-containing molecule that interacts with a number of phosphorylated kinase and receptor molecules including the insulin receptor. Two isoforms of the SH2-B have been identified and have been proposed to arise through alternate splicing. Here we have identified a third isoform of the SH2-B protein, SH2-Bγ, that interacts specifically with the insulin receptor. This interaction required phosphorylation of residue Y1146 in the triple tyrosine motif within the activation loop of the IR kinase and is one of only two signaling molecules shown to interact directly with this residue of the insulin receptor kinase domain. The intron/exon structure of the SH2-B gene was determined. Alternate splice sites utilized to generate the different isoforms of the SH2-B protein were identified in the 3′ end of the SH2-B gene immediately downstream of the exon encoding the core of the SH2 domain. Additionally, the chromosomal location of the SH2-B gene was determined to be the distal arm of mouse Chromosome (Chr) 7 in a region linked to obesity in mice.</abstract><cop>United States</cop><pub>Springer-Verlag</pub><pmid>10594240</pmid><doi>10.1007/s003359901183</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing alternative splicing Alternative Splicing - genetics Amino Acid Sequence Animals Base Sequence Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism chromosome 7 Chromosome Mapping chromosomes Cloning, Molecular exons Exons - genetics genes Insulin insulin receptors introns Introns - genetics Kinases Mice Mice, Inbred C57BL Molecular Sequence Data Molecular Weight obesity Phosphorylation Phosphotyrosine - genetics Phosphotyrosine - metabolism Protein Binding Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism Proteins Receptor, Insulin - chemistry Receptor, Insulin - genetics Receptor, Insulin - metabolism RNA, Messenger - analysis RNA, Messenger - genetics SH2-B gene src Homology Domains - genetics Two-Hybrid System Techniques tyrosine |
| title | Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain |
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