Title : Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity.

Pub. Date : 2011 Aug 19

PMID : 21802411






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity. Methionine holocarboxylase synthetase Homo sapiens
2 HLCS has three putative translational start sites (methionine-1, -7, and -58), but lacks a strong nuclear localization sequence that would explain its participation in epigenetic events in the cell nucleus. Methionine holocarboxylase synthetase Homo sapiens
3 Recent evidence suggests that small quantities of HLCS with a start site in methionine-58 (HLCS58) might be able to enter the nuclear compartment. Methionine holocarboxylase synthetase Homo sapiens
4 First, we generated a novel HLCS fusion protein vector to demonstrate that methionine-58 is a functional translation start site in human cells. Methionine holocarboxylase synthetase Homo sapiens