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dc.contributor.authorForrest, Alistair Raymond Russell
dc.contributor.authorTaylor, Darrin F
dc.contributor.authorCrowe, Mark L
dc.contributor.authorChalk, Alistair M
dc.contributor.authorWaddell, Nic J
dc.contributor.authorKolle, Gabriel
dc.contributor.authorFaulkner, Geoffrey J
dc.contributor.authorKodzius, Rimantas
dc.contributor.authorKatayama, Shintaro
dc.contributor.authorWells, Christine
dc.contributor.authorKai, Chikatoshi
dc.contributor.authorKawai, Jun
dc.contributor.authorCarninci, Piero
dc.contributor.authorHayashizaki, Yoshihide
dc.contributor.authorGrimmond, Sean M
dc.date.accessioned2007-12-03
dc.date.accessioned2017-03-01T20:17:23Z
dc.date.available2017-03-01T20:17:23Z
dc.date.issued2006
dc.date.modified2008-11-25T05:37:31Z
dc.identifier.issn1474-7596
dc.identifier.doihttp://dx.doi.org/10.1186/gb-2006-7-1-r5
dc.identifier.urihttp://hdl.handle.net/10072/20563.1
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 webcite. 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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherBioMed Central Ltd
dc.publisher.placeUnited Kingdom
dc.publisher.urihttp://genomebiology.com/articles/browse.asp
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefromR5
dc.relation.ispartofpagetoR5
dc.relation.ispartofissue1
dc.relation.ispartofjournalGenome Biology
dc.relation.ispartofvolume7
dc.rights.retentionY
dc.subject.fieldofresearchEnvironmental Sciences
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchInformation and Computing Sciences
dc.subject.fieldofresearchcode05
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode08
dc.titleGenome-wide review of transcriptional complexity in mouse protein kinases and phosphatases
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codec1x
gro.facultyEskitis, Inst Cell&Molecular Therapies
gro.date.issued2006
gro.hasfulltextNo Full Text
gro.griffith.authorChalk, Alistair M.


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