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ATR interacting protein (ATRIP) is a conserved regulatory subunit that binds directly to the ATR kinase, forming a heterodimeric complex essential for the DNA damage response in eukaryotic cells[4][5][1][3]. ATRIP localizes ATR to single-stranded DNA (ssDNA) sites coated with replication protein A (RPA), especially during DNA replication stress or after genotoxic damage[1][3]. Through multiple protein-protein interaction domains (including coiled-coil and RPA–ssDNA binding regions), ATRIP facilitates the recognition and signaling of DNA damage, enabling ATR to phosphorylate downstream targets involved in cell cycle arrest, DNA repair, and genome integrity[1][3][2]. Dysfunction or mutations in the ATR–ATRIP pathway are implicated in various cancers and genetic disorders linked to defective DNA repair[2][5][4]. ATRIP is not currently a direct drug target but is critically involved in pathways of clinical interest for cancer therapy through ATR modulation.
Not directly targeted by approved drugs; experimental inhibition or modulation could disrupt DNA damage response
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