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protein and genomic structure of the present day TACC family members suggests that the function of the ancestral TACC protein was mediated solely through the interactions of the conserved TACC domain. Using an in silico protein-protein interaction model based upon known mitotic spindle and centrosomal components, we have previously predicted a number of additional interactions that could be conserved between a functional TACC homologue in yeast, spc-72, and one or more human TACC proteins [21]. Thus, it is known that all the TACC proteins examined to date interact, via the TACC domain, with the microtubule/centrosomal proteins of the stu2/msps/ch-TOG family [5,6,22-24], and with the Aurora kinases [20,21,25]. These interactions are required for the accumulation of the D-TACC, spc72, ceTAC1 and TACC3 proteins to the centrosome [5,6,22-24]. Hence, this functional interaction with the centrosome and mitotic spindle is likely to represent the ancient, conserved function of the TACC family. However, it is apparent that the human TACC proteins also differ in their ability to interact with the Aurora kinases. For instance, TACC1 and TACC3 interact with Aurora A kinase, whereas TACC2 interacts with Aurora C kinase [21], suggesting a degree of functional specialization in the derivatives of the ancestral chordate TACC, after the radiation of the vertebrate TACC genes."}

    craft-ca-core-ex-dev

    {"project":"craft-ca-core-ex-dev","denotations":[{"id":"T7015","span":{"begin":4,"end":11},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7016","span":{"begin":16,"end":23},"obj":"SO_EXT:0001026"},{"id":"T7017","span":{"begin":122,"end":129},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7018","span":{"begin":182,"end":191},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T7019","span":{"begin":197,"end":203},"obj":"SO_EXT:0000417"},{"id":"T7020","span":{"begin":224,"end":231},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7021","span":{"begin":232,"end":239},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7022","span":{"begin":275,"end":282},"obj":"GO:0007067"},{"id":"T7023","span":{"begin":275,"end":290},"obj":"GO:0072686"},{"id":"T7024","span":{"begin":295,"end":306},"obj":"GO:0005813"},{"id":"T7025","span":{"begin":398,"end":407},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T7026","span":{"begin":434,"end":443},"obj":"SO_EXT:0000853"},{"id":"T7027","span":{"begin":447,"end":452},"obj":"NCBITaxon_EXT:yeast"},{"id":"T7028","span":{"begin":454,"end":460},"obj":"PR_EXT:P39723"},{"id":"T7029","span":{"begin":478,"end":483},"obj":"NCBITaxon:9606"},{"id":"T7030","span":{"begin":489,"end":497},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7031","span":{"begin":540,"end":548},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7032","span":{"begin":589,"end":595},"obj":"SO_EXT:0000417"},{"id":"T7033","span":{"begin":606,"end":617},"obj":"GO:0005874"},{"id":"T7034","span":{"begin":618,"end":629},"obj":"GO:0005813"},{"id":"T7035","span":{"begin":630,"end":638},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7036","span":{"begin":646,"end":650},"obj":"PR_EXT:P46675"},{"id":"T7037","span":{"begin":651,"end":655},"obj":"PR_EXT:Q9VEZ3"},{"id":"T7038","span":{"begin":656,"end":662},"obj":"PR_EXT:000005512"},{"id":"T7039","span":{"begin":696,"end":710},"obj":"PR_EXT:000035365"},{"id":"T7040","span":{"begin":703,"end":710},"obj":"GO_EXT:0016301"},{"id":"T7041","span":{"begin":791,"end":796},"obj":"PR_EXT:P39723"},{"id":"T7042","span":{"begin":809,"end":814},"obj":"PR_EXT:000016008"},{"id":"T7043","span":{"begin":815,"end":823},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7044","span":{"begin":831,"end":841},"obj":"GO:0005813"},{"id":"T7045","span":{"begin":899,"end":909},"obj":"GO:0005813"},{"id":"T7046","span":{"begin":914,"end":921},"obj":"GO:0007067"},{"id":"T7047","span":{"begin":914,"end":929},"obj":"GO:0072686"},{"id":"T7048","span":{"begin":966,"end":975},"obj":"SO_EXT:biological_conservation_process_or_quality"},{"id":"T7049","span":{"begin":1038,"end":1043},"obj":"NCBITaxon:9606"},{"id":"T7050","span":{"begin":1049,"end":1057},"obj":"CHEBI_PR_EXT:protein"},{"id":"T7051","span":{"begin":1108,"end":1122},"obj":"PR_EXT:000035365"},{"id":"T7052","span":{"begin":1115,"end":1122},"obj":"GO_EXT:0016301"},{"id":"T7053","span":{"begin":1138,"end":1143},"obj":"PR_EXT:000016006"},{"id":"T7054","span":{"begin":1148,"end":1153},"obj":"PR_EXT:000016008"},{"id":"T7055","span":{"begin":1168,"end":1183},"obj":"PR_EXT:000004515"},{"id":"T7056","span":{"begin":1177,"end":1183},"obj":"GO_EXT:0016301"},{"id":"T7057","span":{"begin":1193,"end":1198},"obj":"PR_EXT:000016007"},{"id":"T7058","span":{"begin":1214,"end":1229},"obj":"PR_EXT:000004518"},{"id":"T7059","span":{"begin":1223,"end":1229},"obj":"GO_EXT:0016301"},{"id":"T7060","span":{"begin":1321,"end":1329},"obj":"NCBITaxon:7711"},{"id":"T7061","span":{"begin":1363,"end":1373},"obj":"NCBITaxon:7742"},{"id":"T7062","span":{"begin":1379,"end":1384},"obj":"SO_EXT:0000704"}],"text":"The protein and genomic structure of the present day TACC family members suggests that the function of the ancestral TACC protein was mediated solely through the interactions of the conserved TACC domain. Using an in silico protein-protein interaction model based upon known mitotic spindle and centrosomal components, we have previously predicted a number of additional interactions that could be conserved between a functional TACC homologue in yeast, spc-72, and one or more human TACC proteins [21]. Thus, it is known that all the TACC proteins examined to date interact, via the TACC domain, with the microtubule/centrosomal proteins of the stu2/msps/ch-TOG family [5,6,22-24], and with the Aurora kinases [20,21,25]. These interactions are required for the accumulation of the D-TACC, spc72, ceTAC1 and TACC3 proteins to the centrosome [5,6,22-24]. Hence, this functional interaction with the centrosome and mitotic spindle is likely to represent the ancient, conserved function of the TACC family. However, it is apparent that the human TACC proteins also differ in their ability to interact with the Aurora kinases. For instance, TACC1 and TACC3 interact with Aurora A kinase, whereas TACC2 interacts with Aurora C kinase [21], suggesting a degree of functional specialization in the derivatives of the ancestral chordate TACC, after the radiation of the vertebrate TACC genes."}

    craft-ca-core-dev

    {"project":"craft-ca-core-dev","denotations":[{"id":"T6914","span":{"begin":16,"end":23},"obj":"SO:0001026"},{"id":"T6915","span":{"begin":197,"end":203},"obj":"SO:0000417"},{"id":"T6916","span":{"begin":275,"end":282},"obj":"GO:0007067"},{"id":"T6917","span":{"begin":275,"end":290},"obj":"GO:0072686"},{"id":"T6918","span":{"begin":295,"end":306},"obj":"GO:0005813"},{"id":"T6919","span":{"begin":434,"end":443},"obj":"SO:0000853"},{"id":"T6920","span":{"begin":454,"end":460},"obj":"PR:P39723"},{"id":"T6921","span":{"begin":478,"end":483},"obj":"NCBITaxon:9606"},{"id":"T6922","span":{"begin":589,"end":595},"obj":"SO:0000417"},{"id":"T6923","span":{"begin":606,"end":617},"obj":"GO:0005874"},{"id":"T6924","span":{"begin":618,"end":629},"obj":"GO:0005813"},{"id":"T6925","span":{"begin":646,"end":650},"obj":"PR:P46675"},{"id":"T6926","span":{"begin":651,"end":655},"obj":"PR:Q9VEZ3"},{"id":"T6927","span":{"begin":656,"end":662},"obj":"PR:000005512"},{"id":"T6928","span":{"begin":696,"end":710},"obj":"PR:000035365"},{"id":"T6929","span":{"begin":791,"end":796},"obj":"PR:P39723"},{"id":"T6930","span":{"begin":809,"end":814},"obj":"PR:000016008"},{"id":"T6931","span":{"begin":831,"end":841},"obj":"GO:0005813"},{"id":"T6932","span":{"begin":899,"end":909},"obj":"GO:0005813"},{"id":"T6933","span":{"begin":914,"end":921},"obj":"GO:0007067"},{"id":"T6934","span":{"begin":914,"end":929},"obj":"GO:0072686"},{"id":"T6935","span":{"begin":1038,"end":1043},"obj":"NCBITaxon:9606"},{"id":"T6936","span":{"begin":1108,"end":1122},"obj":"PR:000035365"},{"id":"T6937","span":{"begin":1138,"end":1143},"obj":"PR:000016006"},{"id":"T6938","span":{"begin":1148,"end":1153},"obj":"PR:000016008"},{"id":"T6939","span":{"begin":1168,"end":1183},"obj":"PR:000004515"},{"id":"T6940","span":{"begin":1193,"end":1198},"obj":"PR:000016007"},{"id":"T6941","span":{"begin":1214,"end":1229},"obj":"PR:000004518"},{"id":"T6942","span":{"begin":1321,"end":1329},"obj":"NCBITaxon:7711"},{"id":"T6943","span":{"begin":1363,"end":1373},"obj":"NCBITaxon:7742"},{"id":"T6944","span":{"begin":1379,"end":1384},"obj":"SO:0000704"}],"text":"The protein and genomic structure of the present day TACC family members suggests that the function of the ancestral TACC protein was mediated solely through the interactions of the conserved TACC domain. Using an in silico protein-protein interaction model based upon known mitotic spindle and centrosomal components, we have previously predicted a number of additional interactions that could be conserved between a functional TACC homologue in yeast, spc-72, and one or more human TACC proteins [21]. Thus, it is known that all the TACC proteins examined to date interact, via the TACC domain, with the microtubule/centrosomal proteins of the stu2/msps/ch-TOG family [5,6,22-24], and with the Aurora kinases [20,21,25]. These interactions are required for the accumulation of the D-TACC, spc72, ceTAC1 and TACC3 proteins to the centrosome [5,6,22-24]. Hence, this functional interaction with the centrosome and mitotic spindle is likely to represent the ancient, conserved function of the TACC family. However, it is apparent that the human TACC proteins also differ in their ability to interact with the Aurora kinases. For instance, TACC1 and TACC3 interact with Aurora A kinase, whereas TACC2 interacts with Aurora C kinase [21], suggesting a degree of functional specialization in the derivatives of the ancestral chordate TACC, after the radiation of the vertebrate TACC genes."}

    2_test

    {"project":"2_test","denotations":[{"id":"15207008-14602875-9666022","span":{"begin":499,"end":501},"obj":"14602875"},{"id":"15207008-12956952-9666023","span":{"begin":671,"end":672},"obj":"12956952"},{"id":"15207008-12956951-9666024","span":{"begin":673,"end":674},"obj":"12956951"},{"id":"15207008-12970190-9666025","span":{"begin":675,"end":677},"obj":"12970190"},{"id":"15207008-12569123-9666025","span":{"begin":675,"end":677},"obj":"12569123"},{"id":"15207008-11433296-9666025","span":{"begin":675,"end":677},"obj":"11433296"},{"id":"15207008-14603251-9666026","span":{"begin":712,"end":714},"obj":"14603251"},{"id":"15207008-14602875-9666027","span":{"begin":715,"end":717},"obj":"14602875"},{"id":"15207008-11827981-9666028","span":{"begin":718,"end":720},"obj":"11827981"},{"id":"15207008-12956952-9666029","span":{"begin":843,"end":844},"obj":"12956952"},{"id":"15207008-12956951-9666030","span":{"begin":845,"end":846},"obj":"12956951"},{"id":"15207008-12970190-9666031","span":{"begin":847,"end":849},"obj":"12970190"},{"id":"15207008-12569123-9666031","span":{"begin":847,"end":849},"obj":"12569123"},{"id":"15207008-11433296-9666031","span":{"begin":847,"end":849},"obj":"11433296"},{"id":"15207008-14602875-9666032","span":{"begin":1231,"end":1233},"obj":"14602875"}],"text":"The protein and genomic structure of the present day TACC family members suggests that the function of the ancestral TACC protein was mediated solely through the interactions of the conserved TACC domain. Using an in silico protein-protein interaction model based upon known mitotic spindle and centrosomal components, we have previously predicted a number of additional interactions that could be conserved between a functional TACC homologue in yeast, spc-72, and one or more human TACC proteins [21]. Thus, it is known that all the TACC proteins examined to date interact, via the TACC domain, with the microtubule/centrosomal proteins of the stu2/msps/ch-TOG family [5,6,22-24], and with the Aurora kinases [20,21,25]. These interactions are required for the accumulation of the D-TACC, spc72, ceTAC1 and TACC3 proteins to the centrosome [5,6,22-24]. Hence, this functional interaction with the centrosome and mitotic spindle is likely to represent the ancient, conserved function of the TACC family. However, it is apparent that the human TACC proteins also differ in their ability to interact with the Aurora kinases. For instance, TACC1 and TACC3 interact with Aurora A kinase, whereas TACC2 interacts with Aurora C kinase [21], suggesting a degree of functional specialization in the derivatives of the ancestral chordate TACC, after the radiation of the vertebrate TACC genes."}