Affinage

TIPIN

TIMELESS-interacting protein · UniProt Q9BVW5

Length
301 aa
Mass
34.6 kDa
Annotated
2026-06-10
30 papers in source corpus 26 papers cited in narrative 26 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TIPIN is a replisome-associated component of the fork protection complex (FPC) that couples DNA unwinding to synthesis and links the replication machinery to checkpoint signaling (PMID:17141802, PMID:19805627). It forms a constitutive heterodimer with TIMELESS (TIM) through composite N-terminal interfaces, and the two proteins mutually stabilize each other's protein level and nuclear localization (PMID:17102137, PMID:17116885, PMID:28334766). At the fork, TIPIN is recruited to RPA-coated ssDNA via a direct interaction between its disordered residues 185-218 and the RPA32 C-terminal domain, which folds into an α-helix upon binding; the resulting Tim-Tipin-RPA assembly is a 1:1:1 heterotrimer that anchors the complex to ssDNA in RPA's compact 30-nt binding mode (PMID:20233725, PMID:20417305, PMID:25348395). Through this anchoring, Tim-Tipin scaffolds Claspin-mediated CHK1 phosphorylation by ATR in response to replication stress and prevents ssDNA accumulation during unperturbed replication, such that ATR-CHK1 signaling becomes indispensable for S-phase progression when the complex is lost (PMID:17102137, PMID:19805627, PMID:20233725). Biochemically, the reconstituted Tim-Tipin complex binds the MCM2-7/CMG helicase and inhibits its ssDNA-dependent ATPase and unwinding activity while stimulating DNA polymerase activity, particularly Pol ε, coupling unwinding to synthesis (PMID:23359676, PMID:23511638). TIPIN additionally promotes Pol α chromatin loading via And1 (and Mta2) and supports establishment of sister chromatid cohesion through cohesin and ChlR1 (PMID:19893489, PMID:20124417, PMID:24830473). Beyond elongation and checkpoint roles, the TIMELESS-TIPIN complex is required for CUL-2LRR-1-mediated CMG ubiquitylation and replisome disassembly at termination (PMID:34269473), and upon DSB induction TIPIN is phosphorylated by ATM to recruit MDC1, promote end resection, and activate NF-κB-dependent anti-apoptotic signaling (PMID:41291151). Loss of TIPIN creates dependence on BRCA1-mediated homologous recombination, manifesting as synthetic lethality rescued by 53BP1 depletion (PMID:39955949).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 2003 Medium

    Establishing TIPIN as a direct TIMELESS partner that controls TIM localization and oligomeric state defined the foundational protein-protein relationship of the complex.

    Evidence Yeast two-hybrid and co-immunoprecipitation with mouse Timeless

    PMID:12875843

    Open questions at the time
    • Functional consequence at replication forks not addressed
    • Interaction interface not mapped
  2. 2006 High

    Defining TIPIN-TIM as a mutually stabilizing, S-phase chromatin-associated complex required for CHK1 phosphorylation connected the heterodimer to the replication checkpoint and genome stability.

    Evidence Co-IP, siRNA knockdown, cell fractionation, and DNA damage response assays in human cells; replisome co-localization and RPA32 binding

    PMID:17102137 PMID:17116885 PMID:17141802

    Open questions at the time
    • Direct mechanism of CHK1 activation not yet defined
    • RPA-binding region of TIPIN not mapped
  3. 2007 High

    Showing RPA-dependent loading of TIPIN onto DNA and its requirement for the UV intra-S checkpoint distinguished TIPIN's checkpoint role from TIM's fork-speed role, revealing non-redundant subunit functions.

    Evidence DNA fiber assays, RPA-coated DNA pulldowns, and siRNA depletion in human cells, plus Xenopus extract depletion/add-back with cyclin E/CDK2 kinase assays

    PMID:17296725 PMID:17846426

    Open questions at the time
    • Molecular basis of RPA-mediated loading unresolved
    • Significance of CDK2 phosphorylation of Tipin unknown
  4. 2009 High

    Identifying And1-dependent Pol α loading and ATR-suppressing ssDNA control placed TIPIN both upstream of checkpoint signaling and within the elongation machinery.

    Evidence Xenopus egg extract depletion, co-IP, and ATR-inhibition epistasis with ssDNA/BrdU readouts

    PMID:19805627 PMID:19893489

    Open questions at the time
    • Direct enzymatic effect on replisome not yet reconstituted
    • Mechanism linking ssDNA suppression to Pol α loading unclear
  5. 2010 High

    Pinpointing the TIPIN-RPA32 interaction as the route to Claspin/CHK1 activation, and mapping cohesin/ChlR1 roles, resolved how the complex transduces checkpoint signals and supports cohesion.

    Evidence In vitro ssDNA-RPA binding, co-IP, cohesion assays, and NMR characterization of TIPIN(185-218)-RPA32C in human cells

    PMID:20124417 PMID:20233725 PMID:20299328 PMID:20417305

    Open questions at the time
    • MCM3-7 interaction (idx 10) rests on a single co-IP without functional follow-up
    • How cohesion and checkpoint functions are coordinated remains open
  6. 2013 High

    Reconstituting Tim-Tipin with purified replisome enzymes demonstrated direct helicase inhibition and polymerase stimulation, establishing the biochemical basis for coupling unwinding to synthesis.

    Evidence Baculovirus-reconstituted complex with in vitro ATPase, unwinding, and polymerase assays

    PMID:23359676 PMID:23511638

    Open questions at the time
    • The two studies disagree on whether Pol α/δ are stimulated
    • TIPIN's individual contribution versus TIM not fully dissected
  7. 2014 High

    Structural and fork-architecture studies (cryo-EM of Tim-Tipin-RPA and reversed-fork/centromere phenotypes) revealed the assembly geometry and showed TIPIN prevents pathological fork remodeling.

    Evidence Cryo-EM 3D reconstruction with AUC, Xenopus extract EM of reversed forks, and TIPIN KO DT40 Top1-collision assays

    PMID:24573676 PMID:24830473 PMID:25348395

    Open questions at the time
    • Atomic-resolution interfaces within the heterotrimer not resolved
    • Role of Mta2/NuRD in Pol α loading mechanistically thin
  8. 2017 High

    Crystal structures of human Timeless N-terminal domain and the yeast Tof1-Csm3 ortholog defined the composite heterodimer interface and a scaffolding alpha-helical architecture with DNA- and Claspin-binding sites.

    Evidence X-ray crystallography with biochemical domain mapping and cross-linking MS

    PMID:28334766 PMID:32469068

    Open questions at the time
    • No full-length Tim-Tipin crystal structure
    • Human TIPIN fold not directly determined
  9. 2021 High

    Demonstrating that TIMELESS-TIPIN is required for CUL-2LRR-1-mediated CMG ubiquitylation extended the complex's role to replication termination and replisome disassembly.

    Evidence In vitro reconstitution and C. elegans RNAi with ubiquitylation assays and synthetic-lethality genetics

    PMID:34269473

    Open questions at the time
    • Mechanism by which the complex recruits CUL-2LRR-1 not defined
    • Conservation of termination role in human cells not directly shown
  10. 2025 Medium

    Connecting ATM-phosphorylated TIPIN to MDC1 recruitment, NF-κB activation, and BRCA1 synthetic lethality positioned TIPIN at the interface of DSB repair, anti-apoptotic signaling, and HR dependence.

    Evidence siRNA, ATM phosphorylation and MDC1 epistasis, NF-κB and caspase assays, and double/triple-mutant chromosomal aberration analysis

    PMID:39955949 PMID:41291151

    Open questions at the time
    • Single-lab findings without independent replication
    • ATM phosphosites on TIPIN not mapped
    • Direct versus indirect role in NF-κB signaling unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • How TIPIN's distinct functions — helicase modulation, checkpoint scaffolding, cohesion, termination, and DSB signaling — are temporally partitioned at a single fork remains unresolved.
  • No high-resolution structure of the full human Tim-Tipin-replisome assembly
  • Regulatory switching between elongation and termination roles unknown
  • TIPIN-specific (versus TIM-dependent) contributions to each function not cleanly separated

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003677 DNA binding 3 GO:0060090 molecular adaptor activity 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0000228 nuclear chromosome 3 GO:0005634 nucleus 3
Pathway
R-HSA-1640170 Cell Cycle 3 R-HSA-69306 DNA Replication 3 R-HSA-73894 DNA Repair 3 R-HSA-8953897 Cellular responses to stimuli 3
Partners
AND1CHLR1CLASPINMCM2-7MDC1MTA2RPA32TIMELESS
Complex memberships
Tim-Tipin fork protection complex (FPC)Tim-Tipin-RPA complexTipin-Tim1-And1 complex

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 TIPIN was identified as a direct binding partner of mouse Timeless (mTIM) via yeast two-hybrid and co-immunoprecipitation. mTIM promotes nuclear localization of TIPIN, and TIPIN disrupts mTIM homo-multimeric complex formation, suggesting TIPIN regulates TIM activity. Yeast two-hybrid, co-immunoprecipitation, transfection/immunofluorescence Journal of molecular biology Medium 12875843
2006 Human TIPIN and Timeless (TIM) interact through the N-terminal segments of each protein and form a stable complex throughout the cell cycle. Loss of either protein reduces the level and nuclear localization of the other, indicating mutual stabilization. Both proteins are found in chromatin-enriched fractions during S phase. Depletion of TIPIN causes radioresistant DNA synthesis and inhibits Chk1 phosphorylation in response to replication stress. TIPIN/TIM may also facilitate nuclear accumulation of Claspin under replication stress. Co-immunoprecipitation, siRNA knockdown, cell fractionation, immunofluorescence The Journal of biological chemistry High 17102137
2006 TIPIN is a nuclear protein that associates with the replicative helicase. TIPIN and Timeless form a complex that maintains the protein levels of both; loss of one leads to loss of the other. TIPIN depletion renders cells sensitive to ionizing radiation and replication stress, causes spontaneous γ-H2AX foci (DSBs), and impairs efficient cell cycle arrest in response to DNA damage. siRNA knockdown, co-immunoprecipitation, immunofluorescence, cell cycle analysis Proceedings of the National Academy of Sciences of the United States of America High 17116885
2006 Mammalian TIM and TIPIN are replisome-associated proteins that co-localize with BrdU-positive replication sites. They interact with components of the endogenous replication fork complex and directly bind the 34 kDa subunit of RPA. TIPIN (ortholog of S. cerevisiae Csm3p / S. pombe Swi3p) and TIM are functional orthologs of replisome-associated yeast counterparts. Co-immunoprecipitation, immunofluorescence, pulldown assays Journal of molecular biology High 17141802
2007 TIPIN interacts with RPA and RPA-coated DNA; RPA promotes loading of TIPIN onto DNA. Depletion of TIPIN reverses the UV-induced intra-S checkpoint (replicon initiation inhibition) and attenuates UV-induced inhibition of DNA chain elongation. Depletion of TIM (but not TIPIN) reduces replication fork progression rate in undamaged cells, indicating distinct roles for each subunit. siRNA knockdown, immunofluorescence of spread DNA fibers (DNA fiber assay), pulldown with RPA-coated DNA Molecular and cellular biology High 17296725
2007 Xenopus Tipin is a substrate of cyclin E/CDK2, phosphorylated in interphase with further phosphorylation upon mitotic entry. Tipin/Tim1 complex is chromatin-bound during unperturbed replication and interacts with the MCM helicase. Depletion of Tipin from Xenopus egg extracts does not significantly impair normal replication but blocks stalled fork recovery after aphidicolin removal, and impairs Chk1 activation and Claspin loading onto chromatin. Xenopus egg extract depletion/reconstitution, in vitro kinase assay, chromatin fractionation, co-immunoprecipitation Proceedings of the National Academy of Sciences of the United States of America High 17846426
2009 In Xenopus egg extracts, Tipin is required for DNA Pol alpha binding to chromatin and interacts with And1, a Pol alpha chromatin-loading factor. Tipin/Tim1/And1 form a complex that promotes stable Pol alpha chromatin binding, DNA replication under origin-limiting conditions, and establishment of sister chromatid cohesion. Xenopus egg extract depletion, co-immunoprecipitation, chromatin fractionation The EMBO journal High 19893489
2009 Tim-Tipin depletion increases ssDNA accumulation at replication forks and stimulates ATR activity during unperturbed DNA replication. Suppression of ATR-Chk1 in Tim-Tipin-deficient cells completely abrogates nucleotide incorporation in S phase, indicating ATR-dependent signaling is indispensable for continued DNA synthesis when Tim-Tipin is absent. The complex prevents ssDNA accumulation upstream of ATR-Chk1 function. siRNA knockdown, BrdU incorporation, immunofluorescence (ssDNA/γ-H2AX), genetic epistasis (ATR inhibition + Tim depletion) The Journal of cell biology High 19805627
2010 The Timeless-Tipin complex mediates Chk1 phosphorylation by ATR specifically through Tipin's interaction with the 34 kDa subunit of RPA (RPA32). The Tipin-RPA interaction stabilizes Timeless-Tipin and Tipin-Claspin complexes on RPA-coated ssDNA, thereby promoting Claspin-mediated phosphorylation of Chk1 by ATR. siRNA knockdown, co-immunoprecipitation, in vitro binding assays with ssDNA-RPA The Journal of biological chemistry High 20233725
2010 Timeless and TIPIN co-purify with cohesin subunits and are required for stable cohesin association with chromatin during S phase. Depletion of Timeless-Tipin impairs sister chromatid cohesion and causes mitotic progression defects. Timeless associates with ChlR1 (cohesion-promoting DNA helicase), and ChlR1 overexpression partially alleviates the cohesion defect caused by Timeless-Tipin depletion. Co-purification/co-immunoprecipitation, siRNA knockdown, chromatin fractionation, chromosome cohesion assay Journal of cell science High 20124417
2010 TIPIN interacts with MCM3-7 proteins (but not MCM2) by co-immunoprecipitation in co-expressed insect cells, consistent with its role at the replication fork. Co-immunoprecipitation in insect cells Journal of biochemistry Low 20299328
2010 The RPA32 C-terminal domain (RPA32C) binds TIPIN(185-218) through a binding interface similar to that used for XPA and UNG2, as characterized by NMR spectroscopy. TIPIN(185-218) is disordered in free state and forms an alpha-helix upon binding RPA32C, using a shared but distinct interaction mode. NMR spectroscopy, in silico modeling The international journal of biochemistry & cell biology Medium 20417305
2011 siRNA-mediated knockdown of TIPIN in human diploid fibroblasts induces a ~4-20 fold increase in sister chromatid discohesion, whereas Timeless knockdown causes ~100-fold increase, indicating Timeless has a SCC function partly independent of the Tim-Tipin complex. Chk1 knockdown does not significantly affect SCC, placing SCC function of Tipin upstream of or independent of Chk1. siRNA knockdown, sister chromatid cohesion assay (cytogenetics), epistasis Cell cycle (Georgetown, Tex.) Medium 21508667
2013 The reconstituted human Tim-Tipin complex directly interacts with Mcm2-7 and Mcm4/6/7 complexes and inhibits their ssDNA-dependent ATPase and DNA unwinding activities. It also inhibits ATPase and helicase activity of the CMG (Cdc45-Mcm2-7-GINS) complex. Tim-Tipin significantly stimulates the polymerase activities of DNA pols α, δ, and ε in vitro; the stimulatory effect on pols and inhibitory effect on MCMs are mediated by distinct regions of Tim protein alone. Baculovirus-reconstituted Tim-Tipin complex, in vitro ATPase assay, DNA unwinding assay, DNA polymerase activity assay, co-immunoprecipitation Proceedings of the National Academy of Sciences of the United States of America High 23359676
2013 Recombinant human Tim-Tipin complex (and Tim alone) directly interacts with DNA polymerase ε by surface plasmon resonance and co-immunoprecipitation, and markedly stimulates Pol ε synthetic activity in vitro. No significant stimulation of Pol α or δ was observed by Tim-Tipin in this study (contrasting with findings in PMID:23359676). Surface plasmon resonance, co-immunoprecipitation, in vitro DNA synthesis assay The Journal of biological chemistry Medium 23511638
2014 In Xenopus egg extracts, Tipin deficiency leads to accumulation of reversed replication fork intermediates. Mta2, a subunit of the NuRD chromatin remodeler complex, was identified as a novel Tipin binding partner; Mta2 is required for Tipin-dependent Pol α binding to replicating chromatin, and this function prevents reversed fork accumulation. Tipin is directly required for efficient replication of vertebrate centromeric DNA. Xenopus egg extract depletion, co-immunoprecipitation, electron microscopy (reversed fork detection), locus-specific replication assay Cell cycle (Georgetown, Tex.) Medium 24830473
2014 In TIPIN knockout DT40 cells, replication fork collisions with CPT-trapped topoisomerase I lead to proteasome-dependent degradation of chromatin-bound Top1, and this is suppressed by aphidicolin pretreatment, indicating that replication forks lacking TIPIN collide at high rate with Top1-DNA adducts. Homologous recombination and replication checkpoint were activated normally in TIPIN KO cells upon CPT treatment. Gene knockout (TIPIN KO DT40 cells), DNA synthesis assay, proteasome inhibitor treatment, aphidicolin epistasis The Journal of biological chemistry Medium 24573676
2014 Cryo-EM structure of the Tim-Tipin-RPA complex reveals a globular 258 kDa heterotrimeric assembly (1:1:1 stoichiometry) with a ring-like and U-shaped domain architecture covered by an RPA lid. RPA in the complex adopts a horseshoe-like conformation resembling its 30-nt ssDNA binding mode. Recruitment of the Tim-Tipin-RPA complex to ssDNA requires RPA to be in the compact 30-nt binding mode. Cryo-EM 3D reconstruction, biochemical complex reconstitution, analytical ultracentrifugation Nucleic acids research High 25348395
2015 TIMELESS forms a physical complex with PARP1 that is distinct from the TIMELESS-TIPIN complex. TIMELESS recruitment to laser-induced DNA damage sites depends on PARP1 binding but not PARP1 catalytic activity. TIMELESS mutants unable to bind PARP1 fail to interact with PARP1 substrates, and TIMELESS knockdown impairs PARP1 substrate recruitment to damage sites and impairs DSB repair. Co-immunoprecipitation, laser micro-irradiation/immunofluorescence, TIMELESS mutant analysis, siRNA knockdown Cell reports Medium 26456830
2017 Crystal structure of the N-terminal domain of human Timeless (residues 1-463) at 1.85 Å resolution reveals a partial binding site for Tipin within this domain. Minimal regions of both Timeless and Tipin required for stable heterodimer formation were defined, showing the Timeless-Tipin interaction is based on a composite binding interface comprising different domains of Timeless. X-ray crystallography, biochemical binding assays, cross-linking mass spectrometry Nucleic acids research High 28334766
2020 Crystal structure of the yeast Tof1-Csm3 (Timeless-Tipin) ortholog complex at 3.1 Å reveals an extended alpha-helical repeat architecture suggesting a mechanical/scaffolding role. A DNA-interacting region and a cancer-associated Mrc1 (Claspin ortholog) binding site were characterized within the complex. X-ray crystallography, biochemical binding characterization Nucleic acids research High 32469068
2020 SDE2 directly interacts with TIMELESS (TIM) and enhances its stability, thereby promoting TIM localization to replication forks and coordination of replisome progression. Loss of SDE2 or TIM results in excessive MRE11-dependent degradation of reversed replication forks, and SDE2 depletion leads to impaired fork progression, stalled fork recovery, and failure to activate CHK1 phosphorylation. Co-immunoprecipitation, siRNA knockdown, DNA fiber assay, chromatin fractionation, MRE11 epistasis Nature communications Medium 33127907
2021 In Caenorhabditis elegans, the TIMELESS-TIPIN complex is required for CUL-2LRR-1 (ubiquitin ligase) recruitment and efficient ubiquitylation of MCM-7 subunit of CMG helicase during replication termination, facilitating replisome disassembly. UBXN-3 (human FAF1) directly stimulates disassembly of ubiquitylated CMG by CDC-48, and co-depletion of UBXN-3 and TIMELESS causes synthetic lethality. In vitro reconstitution, C. elegans in vivo depletion (RNAi), ubiquitylation assays, genetic epistasis (synthetic lethality) The EMBO journal High 34269473
2024 Using proximity ligation assay and colocalization microscopy in human cells, Timeless-Tipin complex remains chromatin-bound and progresses with the replicative helicase (not the blocked polymerase) upon replication stress induced by HU or aphidicolin, indicating spatial dissociation from blocked replication machinery. After stress induction, Timeless interaction with RPA (accumulating on ssDNA) is increased. Proximity ligation assay, colocalization microscopy, chromatin fractionation, replication stress induction Frontiers in cell and developmental biology Medium 38487270
2025 TIPIN and BRCA1 show a synthetic lethal interaction: cells deficient for both accumulate chromosomal aberrations (breaks and radial chromosomes) and die. This synthetic lethality is rescued by depletion of 53BP1, indicating that TIPIN-deficient cells rely on BRCA1-mediated homologous recombination to repair spontaneous DNA lesions. Viability of TIPIN/53BP1/BRCA1 triple mutants is lost by RNF8 depletion, implicating an RNF8-mediated sub-HR pathway as a complementary repair route. Gene knockout (DT40 or similar), genetic epistasis (double/triple mutants), chromosomal aberration analysis Biochemical and biophysical research communications Medium 39955949
2025 TIPIN amplifies ATM signaling in response to topoisomerase inhibitor-induced DSBs and promotes DNA end resection and homology-directed repair. TIPIN is phosphorylated by ATM, and this phosphorylation is required for MDC1 recruitment to stalled forks, which in turn promotes ATM-dependent NF-κB activation, upregulation of anti-apoptotic c-FLIP, and suppression of caspase-8 activation. siRNA knockdown, co-immunoprecipitation, phosphorylation assays, MDC1 depletion epistasis, NF-κB reporter assay, caspase activation assay Communications biology Medium 41291151

Source papers

Stage 0 corpus · 30 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2007 The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement. Molecular and cellular biology 206 17296725
2006 Tipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint function. Proceedings of the National Academy of Sciences of the United States of America 142 17116885
2006 Human Tim/Timeless-interacting protein, Tipin, is required for efficient progression of S phase and DNA replication checkpoint. The Journal of biological chemistry 114 17102137
2006 Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors. Journal of molecular biology 114 17141802
2010 Human Timeless and Tipin stabilize replication forks and facilitate sister-chromatid cohesion. Journal of cell science 113 20124417
2010 Tipin-replication protein A interaction mediates Chk1 phosphorylation by ATR in response to genotoxic stress. The Journal of biological chemistry 104 20233725
2007 Tipin is required for stalled replication forks to resume DNA replication after removal of aphidicolin in Xenopus egg extracts. Proceedings of the National Academy of Sciences of the United States of America 81 17846426
2012 Local and global functions of Timeless and Tipin in replication fork protection. Cell cycle (Georgetown, Tex.) 79 22987152
2009 Tim-Tipin dysfunction creates an indispensible reliance on the ATR-Chk1 pathway for continued DNA synthesis. The Journal of cell biology 79 19805627
2015 TIMELESS Forms a Complex with PARP1 Distinct from Its Complex with TIPIN and Plays a Role in the DNA Damage Response. Cell reports 67 26456830
2009 Tipin/Tim1/And1 protein complex promotes Pol alpha chromatin binding and sister chromatid cohesion. The EMBO journal 66 19893489
2013 Human Tim-Tipin complex affects the biochemical properties of the replicative DNA helicase and DNA polymerases. Proceedings of the National Academy of Sciences of the United States of America 57 23359676
2003 Tipin, a novel timeless-interacting protein, is developmentally co-expressed with timeless and disrupts its self-association. Journal of molecular biology 55 12875843
2020 SDE2 integrates into the TIMELESS-TIPIN complex to protect stalled replication forks. Nature communications 39 33127907
2010 The many facets of the Tim-Tipin protein families' roles in chromosome biology. Cell cycle (Georgetown, Tex.) 38 20139726
2011 Timeless functions independently of the Tim-Tipin complex to promote sister chromatid cohesion in normal human fibroblasts. Cell cycle (Georgetown, Tex.) 30 21508667
2021 TIMELESS-TIPIN and UBXN-3 promote replisome disassembly during DNA replication termination in Caenorhabditis elegans. The EMBO journal 24 34269473
2014 Architecture and ssDNA interaction of the Timeless-Tipin-RPA complex. Nucleic acids research 23 25348395
2010 Interaction of human MCM2-7 proteins with TIM, TIPIN and Rb. Journal of biochemistry 22 20299328
2010 Replication protein A 32 interacts through a similar binding interface with TIPIN, XPA, and UNG2. The international journal of biochemistry & cell biology 21 20417305
2015 TIPIN depletion leads to apoptosis in breast cancer cells. Molecular oncology 19 26004086
2014 Tipin functions in the protection against topoisomerase I inhibitor. The Journal of biological chemistry 16 24573676
2013 The human Tim-Tipin complex interacts directly with DNA polymerase epsilon and stimulates its synthetic activity. The Journal of biological chemistry 16 23511638
2014 Mta2 promotes Tipin-dependent maintenance of replication fork integrity. Cell cycle (Georgetown, Tex.) 15 24830473
2017 Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin. Nucleic acids research 13 28334766
2020 Crystal structure and interactions of the Tof1-Csm3 (Timeless-Tipin) fork protection complex. Nucleic acids research 12 32469068
2020 Knock-down of the TIM/TIPIN complex promotes apoptosis in melanoma cells. Oncotarget 2 32499870
2024 Timeless-Tipin interactions with MCM and RPA mediate DNA replication stress response. Frontiers in cell and developmental biology 1 38487270
2025 TIPIN is essential for chromosome stability and cell viability in BRCA1-deficient cells. Biochemical and biophysical research communications 0 39955949
2025 TIPIN coordinates ATM-dependent checkpoint and NF-κB signaling to counteract DNA replication damage from topoisomerase inhibition. Communications biology 0 41291151

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