Actual CNOT1-family mapping checked against independent human scaffold and repression evidence.

Exact mouse Cnot1 identity and current localization record checked, with the original donor publication inspected.

Exact current donor identities and same-term records inspected; historical family tree, alignment and ancestral placement remain uninspected.

Fetched UniProt nuclear location mapping checked against direct nuclear-receptor and promoter evidence.

Mouse Cnot1 and the recorded Ensembl protein resolve together; the relevant developmental primary study is explicitly mouse/human-model scoped.

Actual ARBA records, mouse identities and relevant current source records inspected, with independent target evidence used to judge biological scope.

Human CNOT1 fragments interact with other CCR4-NOT components.

CNOT1 represses nuclear-receptor-dependent transcription, with positive ER/RXR binding and no measured ligand-dependent RARα interaction.

CNOT1 associates with human CCR4a/b-containing complexes.

The original abstract explicitly reports Tob–Cnot1 interaction in addition to CAF1/CCR4 associations.

Human CCR4-NOT assemblies contain mutually exclusive catalytic subunits and a stable organizing core.

The study inventories membrane-associated proteins from human NK-like cells.

Human Pat1b associates with NOT1 in RNase-resistant coimmunoprecipitation.

Human CNOT1 recruits CAF1 to TTP-targeted reporter mRNAs and promotes deadenylation and decay.

CNOT1 supports complex-associated deadenylase activity, cytoplasmic/P-body localization and P-body abundance.

Human GW182 proteins directly recruit NOT1-containing deadenylase machinery.

Human GW182 motifs recruit CCR4-NOT and can stimulate processive deadenylation.

CNOT1 depletion alters embryonic-stem-cell identity and extraembryonic differentiation markers.

CNOT1 is an enriched protein in the human HeLa mRNA interactome.

CNOT1 is listed in the combined human tear-proteome identification table.

CNOT1 appears among the mRNA-binding candidates from the human-cell capture study.

Human NOT1 directly binds CAF1/POP2 and positions an accessible CAF1 catalytic site.

Human GW182–CNOT1 recruitment contributes to translational repression and miRNA-target decay.

CNOT11 connects an N-terminal CNOT1 module to CNOT10.

GW182 recruitment of CCR4-NOT promotes PABP release from silenced reporter mRNAs.

A human CNOT1 surface binds the TTP C-terminal motif and promotes productive deadenylase recruitment.

Human Nanos motifs bind the CNOT1 SHD and promote translational repression and RNA decay.

CNOT1 binds DDX6 and CNOT9 to connect recruited GW182 proteins to silencing machinery.

TTP, CNOT7 and CNOT1 coimmunoprecipitate in human pulmonary microvascular endothelial cells.

The quantitative HeLa interactome supplies positive CNOT1-associated pairs.

Tagged 4E-T associates with CNOT1-containing repression machinery.

DND1 directly recruits the CNOT1 scaffold and associated CCR4-NOT machinery.

The ISG-interaction dataset includes a positive CNOT1–ANXA2R association.

Defined human CCR4-NOT assemblies coordinate deadenylation through catalytic and nonenzymatic modules.

Human HELZ recruits the NOT module and promotes decay of tethered RNA.

BioPlex provides positive CNOT1-associated pairs in human-cell AP-MS datasets.

The U2OS AP-MS network records CNOT1 associations with CNOT3 and CNOT11.

The actual event, CCR4-NOT complex and CNOT1/A5YKK6 physical-entity chain place CNOT1 in cytosol. Catalytic or BTG2-binding properties of other subunits are not transferred to CNOT1.

The actual event, CCR4-NOT complex and CNOT1/A5YKK6 physical-entity chain place CNOT1 in cytosol. Catalytic or BTG2-binding properties of other subunits are not transferred to CNOT1.

Mouse Cnot1 associates with Nanos2 and localizes to P-bodies in male gonads.

Exact source identities, assay records, target-table entries, product features and access limits are recorded for reproducibility; biological support is provided by primary references.