DAD1

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
DAD1
Identifiers
Aliases DAD1, OST2, defender against cell death 1
External IDs MGI: 101912 HomoloGene: 1027 GeneCards: DAD1
Gene location (Human)
Chromosome 14 (human)
Chr. Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for DAD1
Genomic location for DAD1
Band 14q11.2 Start 22,564,905 bp[1]
End 22,589,269 bp[1]
RNA expression pattern
PBB GE DAD1 200047 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001344

NM_001113358
NM_010015

RefSeq (protein)

NP_001335

NP_001106829
NP_034145

Location (UCSC) Chr 14: 22.56 – 22.59 Mb Chr 14: 54.24 – 54.25 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Dolichyl-diphosphooligosaccharide—protein glycosyltransferase subunit DAD1 is an enzyme that in humans is encoded by the DAD1 gene.[5]

Function[edit]

DAD1, the defender against apoptotic cell death, was initially identified as a negative regulator of programmed cell death in the temperature sensitive tsBN7 cell line. The DAD1 protein disappeared in temperature-sensitive cells following a shift to the nonpermissive temperature, suggesting that loss of the DAD1 protein triggered apoptosis. DAD1 is believed to be a tightly associated subunit of oligosaccharyltransferase both in the intact membrane and in the purified enzyme, thus reflecting the essential nature of N-linked glycosylation in eukaryotes.[5]

Interactions[edit]

DAD1 has been shown to interact with MCL1.[6]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000129562 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022174 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ a b "Entrez Gene: DAD1 defender against cell death 1". 
  6. ^ Makishima T, Yoshimi M, Komiyama S, Hara N, Nishimoto T (September 2000). "A subunit of the mammalian oligosaccharyltransferase, DAD1, interacts with Mcl-1, one of the bcl-2 protein family". J. Biochem. 128 (3): 399–405. doi:10.1093/oxfordjournals.jbchem.a022767. PMID 10965038. 

Further reading[edit]