Werner syndrome ATP-dependent helicase

Werner syndrome
PDB rendering based on 2axl.
Available structures: 2axl, 2dgz, 2e1e, 2e1f, 2fbt, 2fbv, 2fbx, 2fby, 2fc0
Identifiers
Symbol(s)	WRN; RECQL2; RECQL3; DKFZp686C2056; RECQ3
External IDs	OMIM: 604611 MGI: 109635 Homologene: 6659
Gene Ontology Molecular Function: • nucleotide binding • DNA binding • DNA helicase activity • protein binding • ATP binding • ATP-dependent helicase activity • 3'-5' exonuclease activity • hydrolase activity Cellular Component: • intracellular • nucleus Biological Process: • telomere maintenance • DNA recombination • aging • regulation of growth rate
RNA expression pattern
Additional recommended knowledge Guide to balance cleaning: 8 simple steps Safe Weighing Range Ensures Accurate Results Correct Test Weight Handling Guide: 12 Practical Tips More reference expression data
Orthologs
	Human	Mouse
Entrez	7486	22427
Ensembl	ENSG00000165392	ENSMUSG00000031583
Uniprot	Q14191	Q3TB25
Refseq	NM_000553 (mRNA) NP_000544 (protein)	XM_986059 (mRNA) XP_991153 (protein)
Location	Chr 8: 31.01 - 31.15 Mb	Chr 8: 34.7 - 34.85 Mb
Pubmed search	[1]	[2]

WRN (Werner syndrome) is a human gene that provides instructions for producing Werner protein, which is a type of enzyme called a helicase. Helicase enzymes generally unwind and separate double-stranded DNA. These activities are necessary before DNA can be copied in preparation for cell division (DNA replication). Helicase enzymes are also critical for making a blueprint of a gene for protein production, a process called transcription. Further evidence suggests that Werner protein plays a critical role in repairing DNA. Overall, this protein helps maintain the structure and integrity of a person's DNA.

The WRN gene is located on the short (p) arm of chromosome 8 between positions 12 and 11.2, from base pair 31,010,319 to base pair 31,150,818.

Related conditions

Werner syndrome is caused by mutations in the WRN gene. More than 20 mutations in the WRN gene are known to cause Werner syndrome. Many of these mutations result in an abnormally shortened Werner protein. Evidence suggests that the altered protein is not transported into the cell nucleus, where it normally interacts with DNA. This shortened protein may also be broken down too quickly, leading to a loss of Werner protein in the cell. Without normal Werner protein in the nucleus, cells cannot perform the tasks of DNA replication, repair, and transcription. Researchers are still determining how these mutations cause the appearance of premature aging seen in Werner syndrome.

References