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Literature summary extracted from

  • Markolovic, S.; Zhuang, Q.; Wilkins, S.E.; Eaton, C.D.; Abboud, M.I.; Katz, M.J.; McNeil, H.E.; Lesniak, R.K.; Hall, C.; Struwe, W.B.; Konietzny, R.; Davis, S.; Yang, M.; Ge, W.; Benesch, J.L.P.; Kessler, B.M.; Ratcliffe, P.J.; Cockman, M.E.; Fischer, R.; Wappner, P.; Chowdhury, R.; Coleman, M.L.; Schofield, C.J.
    The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases (2018), Nat. Chem. Biol., 14, 688-695 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.11.63
-
 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.63 in presence of Mn2+ and 2-oxoglutarate, to 2.2 A resolution. JMJD7 crystallizes as an oligomer with two or four molecules in each asymmetric unit Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.14.11.63 H178A almost complete loss of activity Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.11.63 cytoplasm
-
 Homo sapiens 5737
-
1.14.11.63 nucleus
-
 Homo sapiens 5634
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.63 a [protein]-L-lysine + 2-oxoglutarate + O2 Drosophila melanogaster
-
 a [protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
-
 ?
1.14.11.63 additional information Drosophila melanogaster enzyme additionally displays slow Fe(II)-stimulated conversion of 2-oxoglutarate to succinate in the absence of a substrate ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.63 Drosophila melanogaster Q9VU77
-
-
1.14.11.63 Homo sapiens P0C870 bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.63 a [protein]-L-lysine + 2-oxoglutarate + O2
-
 Drosophila melanogaster a [protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
-
 ?
1.14.11.63 additional information enzyme additionally displays slow Fe(II)-stimulated conversion of 2-oxoglutarate to succinate in the absence of a substrate Drosophila melanogaster ?
-
 ?
1.14.11.63 additional information enzyme additionally displays slow Fe(II)-stimulated conversion of 2-oxoglutarate to succinate in the absence of a substrate Homo sapiens ?
-
 ?
1.14.11.63 [protein]-L-lysine + 2-oxoglutarate + O2 substrate is Developmentally Regulated GTP Binding Protein 1 Homo sapiens [protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
-
 ?
1.14.11.63 [protein]-L-lysine + 2-oxoglutarate + O2 substrate is Developmentally Regulated GTP Binding Protein 2 Homo sapiens [protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.11.63 JMJD7
-
 Drosophila melanogaster
1.14.11.63 JMJD7
-
 Homo sapiens
1.14.11.63 Jumonji domain-containing protein 7
-
 Drosophila melanogaster
1.14.11.63 Jumonji domain-containing protein 7
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.14.11.63 physiological function enzyme interacts with Developmentally Regulated GTP Binding Proteins 1 and 2, DRG1/2 Homo sapiens
1.14.11.63 physiological function knockdown of JMJD7 correlates with increased posterior wing compartment size, likely through an increase in cell size Drosophila melanogaster