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dc.contributor.authorForrest, Alistairen_US
dc.contributor.authorTaylor, Darrinen_US
dc.contributor.authorCrowe, Marken_US
dc.contributor.authorChalk, Alistairen_US
dc.contributor.authorWaddell, Nicen_US
dc.contributor.authorKolle, Gabrielen_US
dc.contributor.authorFaulkner, Geoffreyen_US
dc.contributor.authorKodzius, Rimantasen_US
dc.contributor.authorKatayama, Shintaroen_US
dc.contributor.authorWells, Christineen_US
dc.contributor.authorKai, Chikatoshien_US
dc.contributor.authorKawai, Junen_US
dc.contributor.authorCarninci, Pieroen_US
dc.contributor.authorHayashizaki, Yoshihideen_US
dc.contributor.authorGrimmond, Seanen_US
dc.date.accessioned2017-05-03T15:23:17Z
dc.date.available2017-05-03T15:23:17Z
dc.date.issued2006en_US
dc.date.modified2010-08-26T07:36:59Z
dc.identifier.issn14656914en_US
dc.identifier.doi10.1186/gb-2006-7-1-r5en_AU
dc.identifier.urihttp://hdl.handle.net/10072/25134
dc.description.abstractBackground Alternative transcripts of protein kinases and protein phosphatases are known to encode peptides with altered substrate affinities, subcellular localizations, and activities. We undertook a systematic study to catalog the variant transcripts of every protein kinase-like and phosphatase-like locus of mouse http://variant.imb.uq.edu.au. Results By reviewing all available transcript evidence, we found that at least 75% of kinase and phosphatase loci in mouse generate alternative splice forms, and that 44% of these loci have well supported alternative 5' exons. In a further analysis of full-length cDNAs, we identified 69% of loci as generating more than one peptide isoform. The 1,469 peptide isoforms generated from these loci correspond to 1,080 unique Interpro domain combinations, many of which lack catalytic or interaction domains. We also report on the existence of likely dominant negative forms for many of the receptor kinases and phosphatases, including some 26 secreted decoys (seven known and 19 novel: Alk, Csf1r, Egfr, Epha1, 3, 5,7 and 10, Ephb1, Flt1, Flt3, Insr, Insrr, Kdr, Met, Ptk7, Ptprc, Ptprd, Ptprg, Ptprl, Ptprn, Ptprn2, Ptpro, Ptprr, Ptprs, and Ptprz1) and 13 transmembrane forms (four known and nine novel: Axl, Bmpr1a, Csf1r, Epha4, 5, 6 and 7, Ntrk2, Ntrk3, Pdgfra, Ptprk, Ptprm, Ptpru). Finally, by mining public gene expression data (MPSS and microarrays), we confirmed tissue-specific expression of ten of the novel isoforms. Conclusion These findings suggest that alternative transcripts of protein kinases and phosphatases are produced that encode different domain structures, and that these variants are likely to play important roles in phosphorylation-dependent signaling pathways.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.format.extent1168101 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherBioMed Central Ltden_US
dc.publisher.placeEnglanden_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefromR5.1en_US
dc.relation.ispartofpagetoR5.15en_US
dc.relation.ispartofissue1en_US
dc.relation.ispartofjournalGenome Biologyen_US
dc.relation.ispartofvolume7en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchcode279999en_US
dc.titleGenome-wide review of transcriptional complexity in mouse protein kinases and phosphatasesen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
dcterms.licensehttp://creativecommons.org/licenses/by/2.0en_US
gro.rights.copyrightCopyright [2006] [Chalk] et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.en_AU
gro.date.issued2006
gro.hasfulltextFull Text


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