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ProteomicsMapping of ATR–ATRIP phosphorylation sites before and after autophosphorylation
ATR–ATRIP is activated upon binding to TopBP1, and this activation is driven by TopBP1-mediated autophosphorylation. To identify the phosphorylation sites associated with ATR–ATRIP activation, we prepared ATR–ATRIP samples before and after autophosphorylation and performed nano-HPLC–MS/MS analysis t...
ORGANISM(S): Mus musculus (Mouse) 
2026-08-18 | PXD082486 | Pride
Phosphorylation sites Activation Atr-atrip 
UnknownCryo-EM structure of human ATR-ATRIP complex.
Not available
S-EPMC5799817 | biostudies-literature
UnknownREV7 associates with ATRIP and inhibits ATR kinase activity.
Not available
S-EPMC12820532 | biostudies-literature
UnknownATRIP Deacetylation by SIRT2 Drives ATR Checkpoint Activation by Promoting Binding to RPA-ssDNA.
Not available
S-EPMC4758896 | biostudies-literature
UnknownAPE1 recruits ATRIP to ssDNA in an RPA-dependent and -independent manner to promote the ATR DNA damage response.
Not available
S-EPMC10202453 | biostudies-literature
UnknownA novel interplay between the Fanconi anemia core complex and ATR-ATRIP kinase during DNA cross-link repair.
Not available
S-EPMC3737553 | biostudies-literature
UnknownA kinase-independent role for the Rad3(ATR)-Rad26(ATRIP) complex in recruitment of Tel1(ATM) to telomeres in fission yeast.
Not available
S-EPMC2816689 | biostudies-literature
ProteomicsREV7 associates with ATRIP and FAM35A
REV7 is a remarkably multi-faceted protein with important and separable roles in multiple genome maintenance pathways including Trans-Lesion Synthesis, the Fanconi Anemia pathway, as well as p53 signaling and Double Stranded Break resection. To investigate novel functions and pathways involving REV7...
ORGANISM(S): Homo sapiens (Human) 
2026-01-22 | PXD072142 | Pride
Atrip Rev7 Fam35a 
ProteomicsSystem-wide analysis of SUMOylation dynamics in response to replication stress reveals novel SUMO target proteins and acceptor lysines relevant for genome stability
Genotoxic agents can cause replication fork stalling in dividing cells due to DNA lesions, eventually leading to replication fork collapse when the damage is not repaired. Small Ubiquitin-like Modifiers (SUMOs) are known to counteract replication stress, nevertheless, only a small number of relevant...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080851 | MassIVE
Proteomicsβ-tubulin phosphorylation by Chk1 is required for normal spindle formation during cell division
The mitotic spindle is a microtubule-based apparatus that is responsible for accurate segregation of chromosomes into two daughter cells. In this study, we show that the DNA damage kinase Chk1 is required for optimal density and efficient polymerization of spindle microtubules during unperturbed mit...
ORGANISM(S): Homo sapiens (Human) Spodoptera frugiperda 
2026-06-08 | PXD074543 | Pride
Atr Atrip Topbp1 Centrosome Chromosome segregation -tubulin Chk1 Cell proliferation Mitotic spindle 
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