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ATRIP encodes an essential component of the DNA damage checkpoint. Additionally we are shipping ATRIP Antibodies (108) and ATRIP Kits (8) and many more products for this protein.
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ATRIP must associate with ATR in order for ATR to carry out the phosphorylation of Chk1 (show CHEK1 Proteins) effectively
Data show that recombinant TopBP1 (show TOPBP1 Proteins) induces a large increase in the kinase activity of both Xenopus and human ATR-ATRIP.
ATRIP SUMOylation promotes ATR activation by providing a unique type of protein glue that boosts multiple protein interactions along the ATR pathway
Data on crystal structure of BRCA1 binding with phosphopeptides suggest that C-terminal domain of BRCA1 interacts with ATRIP and BAAT1 (show C7orf27 Proteins) with preferences for specific side chains; in ATRIP, phospho-Ser239 and Phe242 are the main interacting residues.
Data indicate that ATRIP is a direct target gene of HIF-1, and the increased ATRIP then activates the ATR signaling pathway under hypoxia.
our analysis exposes an overlapping clinical manifestation between the disorders but allows an expanded spectrum of clinical features for ATR (show ANTXR1 Proteins)-ATRIP Seckel Syndrome to be defined
as an ATR (show ANTXR1 Proteins)-associated kinase, Nek1 (show NEK1 Proteins) enhances the stability and activity of ATR (show ANTXR1 Proteins)-ATRIP before DNA damage, priming ATR (show ANTXR1 Proteins)-ATRIP for a robust DNA damage response
ATRIP may function outside the context of the canonical ATR damage signaling pathway during HSV-1 infection to participate in the viral life cycle.
data suggest that RPA (show RPA1 Proteins)-coated ssDNA is the critical structure at sites of DNA damage that recruits the ATR (show ANTXR1 Proteins)-ATRIP complex and facilitates its recognition of substrates for phosphorylation and the initiation of checkpoint signaling
there are at least two in vitro ATR-ATRIP DNA binding complexes, one which binds DNA with high affinity in an RPA-dependent manner and a second, which binds DNA with lower affinity in an RPA-independent manner
Collectively, our results suggest that the ATR (show ANTXR1 Proteins)-mediated phosphorylation of ATRIP at Ser (show SIGLEC1 Proteins)-68 and -72 is dispensable for the initial response to DNA damage.
N-terminal domain of the ATRIP protein contributes to the cell cycle checkpoint by regulating the intranuclear localization of ATR
This gene encodes an essential component of the DNA damage checkpoint. The encoded protein binds to single-stranded DNA coated with replication protein A. The protein also interacts with the ataxia telangiectasia and Rad3 related protein kinase, resulting in its accumulation at intranuclear foci induced by DNA damage. Multiple transcript variants encoding different isoforms have been found for this gene.
, three prime repair exonuclease 1
, ATR interacting protein
, ATR-interacting protein-like
, mutagen sensitive 304
, ATM and Rad3-related-interacting protein
, ATM and Rad3 related interacting protein