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Literature summary for 1.14.11.4 extracted from

  • Mantri, M.; Webby, C.; Loik, N.; Hamed, R.; Nielsen, M.; McDonough, M.; McCullagh, J.; Boettger, A.; Schofield, C.; Wolf, A.
    Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6 (2012), MedChemComm, 3, 80-85.
No PubMed abstract available
Search for more literature for 1.14.11.4

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ dependent on Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine-[procollagen] + 2-oxoglutarate + O2 Homo sapiens
-
 (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
 ?
additional information Homo sapiens JMJD6 undergoes self-hydroxylation in the presence of Fe(II) and 2-oxoglutarate, in absence of substrate or in presence of substrates like U2AF65, resulting in production of (5S)<-hydroxylysine residues. JMJD6 in human cells is hydroxylated ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine-[procollagen] + 2-oxoglutarate + O2
-
 Homo sapiens (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2
-
 ?
additional information JMJD6 undergoes self-hydroxylation in the presence of Fe(II) and 2-oxoglutarate, in absence of substrate or in presence of substrates like U2AF65, resulting in production of (5S)<-hydroxylysine residues. JMJD6 in human cells is hydroxylated Homo sapiens ?
-
 ?
additional information in absence of substrate JMJD6 catalyses turnover of 2-oxoglutarate to succinate Homo sapiens ?
-
 ?
U2AF65 + 2-oxoglutarate + O2
-
 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
Jmjd6
-
 Homo sapiens
lysyl 5S-hydroxylase
-
 Homo sapiens
lysyl hydroxylase
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function the lysyl 5S-hydroxylase, JMJD6 acts on proteins involved in RNA splicin. JMJD6 in human cells is self-hydroxylated at Lys111JMJD6 and Lys167JMJD6 to give lysyl 5S-hydroxylase. Self-hydroxylation of JMJD6 may play a regulatory role in modulating the hydroxylation status of proteins involved in RNA splicing Homo sapiens