Literature summary for 3.1.21.10 extracted from

Rass, U.; Compton, S.A.; Matos, J.; Singleton, M.R.; Ip, S.C.; Blanco, M.G.; Griffith, J.D.; West, S.C.
Mechanism of Holliday junction resolution by the human GEN1 protein (2010), Genes Dev., 24, 1559-1569.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	substrate specificity of GEN1, and GEN1-Holliday junction complex structures, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	substrate specificity of GEN1, and GEN1-Holliday junction complex structures, overview	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
monomer	GEN1 protein contains the XPG-N, XPG-I, and helix-hairpin-helix domains essential for nuclease activity, linked to a C-terminal tail region that appears to be naturally disordered	Homo sapiens

Synonyms

Synonyms	Comment	Organism
GEN1 protein	-	Homo sapiens
More	GEN1 is a member of the Rad2/XPG nuclease family	Homo sapiens

General Information

General Information	Comment	Organism
additional information	GEN1 is a monomeric 5'-flap endonuclease. The unique feature of GEN1 that distinguishes it from other Rad2/XPG nucleases is its ability to dimerize on Holliday junctions	Homo sapiens
physiological function	Holliday junction resolution is essential for chromosome segregation at meiosis and the repair of stalled/collapsed replication forks in mitotic cells. Resolution by introduction of symmetrically related nicks in two strands at, or close to, the junction point. Structural basis and mechanism of Holliday junction resolution by the human GEN1 protein, overview	Homo sapiens

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Release 2023.1 (January 2023)