background:
EME1 complexes with methyl methanesulfonate-sensitive USLVsensitive 81 protein (MUS81) to form an endonuclease complex which cleaves branched DNA structures, especially those arising during stalled DNA replication. The protein may be involved in repairing DNA damage and in maintaining genomic stability. It interacts with specifc DNA structures including nicked Holliday junctions, 3'-flap structures and aberrant replication fork structures. Alternative splicing results in multiple transcript variants.
Function:
Interacts with MUS81 to form a DNA structure-specificendonuclease with substrate preference for branched DNA structureswith a 5'-end at the branch nick. Typical substrates include3'-flap structures, replication forks and nicked Hollidayjunctions. May be required in mitosis for the processing of stalledor collapsed replication forks.
Subunit:
May self-associate. Interacts with MUS81. Interacts withERCC4 and FANCM.
Subcellular Location:
Nucleus, nucleolus. Note=Recruited toregions of DNA damage in S-phase cells.
Similarity:
Belongs to the EME1/MMS4 family.
Database links:
UniProtKB/Swiss-Prot: Q96AY2.2
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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