1.14.11.63: peptidyl-lysine (3S)-dioxygenase
This is an abbreviated version!
For detailed information about peptidyl-lysine (3S)-dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.63
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1.14.11.63
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histone
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demethylases
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trafac
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jumonji-c
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jarid2
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prdm10
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hif1an
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clipping
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gametogenesis
- 1.14.11.63
- histone
- demethylases
-
trafac
-
jumonji-c
- jarid2
-
prdm10
-
hif1an
-
clipping
-
gametogenesis
Reaction
Synonyms
JmjC domain-containing protein 7, JMJD7, Jumonji domain-containing protein 7
ECTree
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General Information
General Information on EC 1.14.11.63 - peptidyl-lysine (3S)-dioxygenase
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physiological function
enzyme interacts with Developmentally Regulated GTP Binding Proteins 1 and 2, DRG1/2
physiological function
knockdown of JMJD7 correlates with increased posterior wing compartment size, likely through an increase in cell size
physiological function
the content of arginine methylation of both histones H3R2/H4R3 and overall H3/H4 is increased with the knockout of JMJD7, and the colony-forming abilities of JMJD7-deficient MDA-MB-231 cells are greatly decreased
physiological function
JMJD5, EC 1.14.11.73, and JMJD7 function as endopeptidases that cleave histone tails specifically adjacent to methylated arginine residues and continue to degrade N-terminal residues of histones via their aminopeptidase activity. Recognition between the enzymes and histone substrates is specific. JMJD5 and JMJD7 show high structural similarity, share common substrates and high binding affinity. JMJD5 does not bind to arginine methylated histone tails with additional lysine acetylation while JMJD7 does not bind to arginine methylated histone tails with additional lysine methylation