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dc.contributor.authorEisenhaber, Birgit-
dc.contributor.authorSinha, Swati-
dc.contributor.authorJadalanki, Chaitanya K.-
dc.contributor.authorShitov, Vladimir A.-
dc.contributor.authorTan, Qiao Wen-
dc.contributor.authorSirota, Fernanda L.-
dc.contributor.authorEisenhaber, Frank-
dc.date.accessioned2022-06-25T06:33:37Z-
dc.date.available2022-06-25T06:33:37Z-
dc.date.issued2021-01-12-
dc.identifier.urihttps://doi.org/10.1186/s13062-021-00291-w-
dc.identifier.urihttp://hdl.handle.net/20.500.12701/2148-
dc.description.abstractThe human proteins TMTC1, TMTC2, TMTC3 and TMTC4 have been experimentally shown to be components of a new O-mannosylation pathway. Their own mannosyl-transferase activity has been suspected but their actual enzymatic potential has not been demonstrated yet. So far, sequence analysis of TMTCs has been compromised by evolutionary sequence divergence within their membrane-embedded N-terminal region, sequence inaccuracies in the protein databases and the difficulty to interpret the large functional variety of known homologous proteins (mostly sugar transferases and some with known 3D structure).ru_RU
dc.language.isoenru_RU
dc.publisherBioMed Central Ltdru_RU
dc.relation.ispartofseriesBiology Direct;Volume 16, Issue 4-
dc.subjectTMTC1ru_RU
dc.subjectTMTC2ru_RU
dc.subjectTMTC3ru_RU
dc.subjectTMTC4ru_RU
dc.subjectPMTru_RU
dc.subjectDolichyl-phosphate-mannose-protein mannosyltransferaseru_RU
dc.subjectGT-C glycosyl transferaseru_RU
dc.subjectO-mannosylationru_RU
dc.subjectMembrane topologyru_RU
dc.subjectTransmembrane region predictionru_RU
dc.titleConserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sitesru_RU
dc.typeArticleru_RU
Располагается в коллекциях:Biology Direct

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