ERCC6

Summary: CSB contributes to cellular single-strand-break repair under alkylation stress.

Reason: PMID:29545921 Figure1 and the associated Results compare human CS-B fibroblasts, controls and wild-type-complemented cells by alkaline comet assays after MMS, including G1-enriched cells. Delayed disappearance of strand breaks supports a contextual repair contribution. Retain this existing assertion as non-core without assigning CSB a glycosylase, end-processing or ligase reaction, or treating the comet endpoint as identification of a particular chemical step.

Summary: CSB supports the DNA-damage checkpoint in the tested human-cell context.

Reason: PMID:25820262 Results/Figures2–8 use human hTERT-RPE CSB knockout and rescue, checkpoint/ATM–Chk2 measurements and repair reporters. These support a positive checkpoint contribution in addition to the chromatin-remodeling role. This contextual regulatory function does not make CSB the checkpoint kinase.

Summary: The directly tested DNA ligand is double-stranded DNA.

Reason: PMID:12560492 Methods89–129 and Results/Table2/Figures2–6 measure purified human CSB binding to a 166-bp duplex by filter binding. The ATPase-defective E646Q retains binding, distinguishing ligand binding from hydrolysis. Refine the broad DNA term to the measured duplex ligand.

Proposed replacements: double-stranded DNA binding

Summary: Independent purified-human-CSB experiments establish duplex DNA binding.

Reason: PMID:16107709 Table1 summarizes earlier DNA-binding measurements; its operative experiments primarily examine PARP1 interaction and inhibition of CSB ATPase. The precise binding claim is independently established by PMID:12560492 Table2 and PMID:8999876 Figure3 with purified human CSB and duplex DNA. Refine to double-stranded DNA binding while retaining that source distinction.

Proposed replacements: double-stranded DNA binding

Summary: Purified human CSB binds duplex DNA.

Reason: PMID:8999876 Methods and Figure3 directly assay binding of purified full-length human CSB to a 90-bp duplex. Refine the broad DNA term; this is separate from ATP hydrolysis and from the negative strand-unwinding result in the same paper.

Proposed replacements: double-stranded DNA binding

Summary: Preserve the experimentally supported NOT DNA-helicase annotation.

Reason: This source row is negated. PMID:8999876 Figure4 and operative Results test purified human CSB on a partial duplex, with positive UvrD control and assays with CSA, without detecting strand displacement. The result is compatible with ATP-dependent DNA translocation rather than helicase unwinding. Accept the negative assertion within the tested conditions, without claiming that every possible substrate/context was excluded.

Summary: SUMO-associated human CSB is recovered in the chromatin fraction.

Reason: PMID:26620705 Methods and Figure4C distinguish Triton-soluble and chromatin-associated fractions of human cells expressing CSB variants. The SUMO-modified CSB species associates with chromatin after UV. This directly supports chromatin binding in the tested cellular context; it does not establish sequence-specific DNA recognition.

Summary: CSB associates with damaged chromatin in human cells.

Reason: PMID:25820262 Results and chromatin-fractionation experiments show human CSB recruitment after DNA damage. The W851R ATPase-defective variant can still associate with chromatin, separating localization/binding from downstream motor-dependent repair effects.

Summary: CSB associates with XAB2 in a human nuclear assembly.

Reason: PMID:10944529 Methods and Figure5 use functional tagged human CSB in CS1AN-SV cells, anti-tag immunoprecipitation and fractionation to detect XAB2/CSB association. This supports the imported XAB2 partner context but is not a purified binary CSB–XAB2 interaction assay. Retain the supported generic binding assertion as non-core.

Summary: Purified human CSB binds PARP1.

Reason: PMID:16107709 Methods and Figures1–3 demonstrate CSB–PARP1 association by purified-protein ELISA/immunoprecipitation with DNA-removal controls and N-terminal mapping. The relationship is supported, but the paper does not show that CSB activates PARP1; PARP1 modification instead inhibits CSB ATPase in the tested system. Retain binding as non-core.

Summary: Human CSB directly interacts with the XPG C-terminal region.

Reason: PMID:16246722 Methods and Figure4 combine purified human proteins, far-western interaction mapping, DNA-bubble binding and ATPase assays. XPG stimulates CSB ATPase preferentially on a bubble substrate. This supports the imported XPG interaction; the separate TFIIH-dependent polymerase-remodeling experiment is not attributed to CSB. Retain the generic interaction as non-core.

Summary: The experimentally identified ligand is the ABL1 protein tyrosine kinase.

Reason: PMID:17626041 Methods and Figures1–2 establish CSB–ABL1 association with recombinant interaction mapping involving the CSB proline-rich region and ABL SH3 domain, alongside cellular evidence. Replace generic binding with the current specific protein-tyrosine-kinase-binding term. This does not make CSB a kinase.

Proposed replacements: protein tyrosine kinase binding

Summary: UVSSA and CSB occur in the UV-induced human transcription-repair assembly.

Reason: PMID:22466612 was verified at the publisher, but its operative Methods/Results were not recovered. Independently read PMID:32355176 Figure5b/c shows human GFP–UVSSA pull-down/co-IP containing CSB after UV, and PMID:34526721 resolves the shared repair assembly. These establish the biological interaction while leaving the exact original experiment unverified. Retain generic binding as non-core; do not describe it as an isolated binary binding measurement.

Summary: Human CSB associates with a SMARCB1-containing BAF assembly.

Reason: PMID:24874740 uses near-endogenous human CSB-TAP and cellular interaction experiments together with BAF recruitment analyses. The SMARCB1 partner assertion is supported at the complex level; no purified binary CSB–SMARCB1 affinity measurement is claimed. Keep the interaction as non-core.

Summary: Human CSB associates with PSMD12 in tagged-protein co-immunoprecipitation (anti-Flag capture only).

Reason: PMID:26030138 Figure 6D tests human CSB-Flag and PSMD12-Myc in CS1AN fibroblast lysates. Anti-Flag capture recovered the partner; the reciprocal anti-Myc experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone. S1 Table row 18 reports 2 control versus 6 CSB-TAP unique peptides for this partner, so the original screen is not described as complete absence from the control.

Summary: Human CSB associates with DDX3X in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4C tests human CSB-Flag and DDX3X-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with PRPF4 in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5G tests human CSB-Flag and PRPF4-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone. S1 Table row 26 reports 1 control versus 5 CSB-TAP unique peptides for this partner, so the original screen is not described as complete absence from the control.

Summary: Human CSB associates with PSMD3 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4L tests human CSB-Flag and PSMD3-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with PRPF3 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4K tests human CSB-Flag and PRPF3-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with MTA2 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4J tests human CSB-Flag and MTA2-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with TOP1 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4Q tests human CSB-Flag and TOP1-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with TOP2A in tagged-protein co-immunoprecipitation (anti-Flag capture only).

Reason: PMID:26030138 Figure 6E tests human CSB-Flag and TOP2A-Myc in CS1AN fibroblast lysates. Anti-Flag capture recovered the partner; the reciprocal anti-Myc experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with XRCC5 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4S tests human CSB-Flag and XRCC5-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with DDX5 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4D tests human CSB-Flag and DDX5-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone. S1 Table row 7 reports 1 control versus 13 CSB-TAP unique peptides for this partner, so the original screen is not described as complete absence from the control.

Summary: Human CSB associates with SFPQ in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4N tests human CSB-Flag and SFPQ-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with SMARCA1 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4O tests human CSB-Flag and SMARCA1-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with SMARCA2 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4P tests human CSB-Flag and SMARCA2-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone. Figure 4T–U includes unfused-tag negative controls for the weak reciprocal bands.

Summary: Human CSB associates with PSMC5 in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5H tests human CSB-Flag and PSMC5-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with HNRNPU in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4I tests human CSB-Flag and HNRNPU-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with CSTF1 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4B tests human CSB-Flag and CSTF1-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with RBBP4 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4M tests human CSB-Flag and RBBP4-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with SF3B2 in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5I tests human CSB-Flag and SF3B2-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone. S1 Table row 6 reports 1 control versus 15 CSB-TAP unique peptides for this partner, so the original screen is not described as complete absence from the control.

Summary: Human CSB associates with HDAC1 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4H tests human CSB-Flag and HDAC1-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with NONO in tagged-protein co-immunoprecipitation (anti-Flag capture only).

Reason: PMID:26030138 Figure 6C tests human CSB-Flag and NONO-Myc in CS1AN fibroblast lysates. Anti-Flag capture recovered the partner; the reciprocal anti-Myc experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with CTR9 in tagged-protein co-immunoprecipitation (anti-Flag capture only).

Reason: PMID:26030138 Figure 6A tests human CSB-Flag and CTR9-Myc in CS1AN fibroblast lysates. Anti-Flag capture recovered the partner; the reciprocal anti-Myc experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with COPS6 in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5C tests human CSB-Flag and COPS6-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with CAND1 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4A tests human CSB-Flag and CAND1-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with GATAD2A in tagged-protein co-immunoprecipitation (anti-Flag capture only).

Reason: PMID:26030138 Figure 6B tests human CSB-Flag and GATAD2A-Myc in CS1AN fibroblast lysates. Anti-Flag capture recovered the partner; the reciprocal anti-Myc experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with GATAD2B in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5F tests human CSB-Flag and GATAD2B-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with DDX1 in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5D tests human CSB-Flag and DDX1-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with DDX17 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4E tests human CSB-Flag and DDX17-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone. The p72/p82 bands in Figure 4E are DDX17 alternative translation products, not CSB or CSB–PGBD3 isoforms.

Summary: Human CSB associates with USP7 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4R tests human CSB-Flag and USP7-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with COPS4 in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5B tests human CSB-Flag and COPS4-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with DDX23 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4F tests human CSB-Flag and DDX23-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with DHX36 in tagged-protein co-immunoprecipitation (both reciprocal immunoprecipitation directions).

Reason: PMID:26030138 Figure 4G tests human CSB-Flag and DHX36-Myc in CS1AN fibroblast lysates. Anti-Myc and anti-Flag capture each recovered the other tagged protein. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: Human CSB associates with DDX41 in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5E tests human CSB-Flag and DDX41-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone. S1 Table row 19 reports 1 control versus 6 CSB-TAP unique peptides for this partner, so the original screen is not described as complete absence from the control.

Summary: Human CSB associates with COPS3 in tagged-protein co-immunoprecipitation (anti-Myc capture only).

Reason: PMID:26030138 Figure 5A tests human CSB-Flag and COPS3-Myc in CS1AN fibroblast lysates. Anti-Myc capture recovered CSB; the reciprocal anti-Flag experiment did not confirm this association. The preceding full-length CSB-TAP screen used a TAP-only control and a clone that restored UV survival, but the interaction assays were performed without exogenous DNA damage. These are cellular association assays, not purified binary-binding or catalytic tests; they do not establish that CSB performs the partner's molecular activity. Retain the supported generic interaction as non-core; no more specific molecular function is assigned from complex co-recovery alone.

Summary: CSB associates with the assayed Elongin A construct.

Reason: PMID:28292928 Methods and Figures1–3 use human CSB with a rat Elongin A construct in human U2OS/CS1AN cells. AP-FRET and CSB-dependent recruitment support the imported rat Q63187 partner context. Preserve the actual organism/construct boundary and retain this interaction as non-core rather than relabeling the assayed partner as human.

Summary: CSB associates with the CUL5-containing elongation-factor assembly.

Reason: PMID:28292928 Figures1–3 and Methods use human-cell AP-FRET and damage recruitment, with inducible CSB rescue, to connect CSB with Elongin A/CUL5. This is supported cellular association and recruitment, not an isolated binary binding or CSB ubiquitin-ligase assay. Keep the CUL5 interaction as non-core.

Summary: Human CSB associates with RIF1 during the double-strand-break response.

Reason: PMID:29203878 Results/Figure1 use reciprocal endogenous immunoprecipitation in HCT116 cells; tethering experiments further map the CSB C-terminal interaction to the RIF1 C-terminal region. Retain this supported contextual interaction as non-core, without converting phosphorylation of CSB by upstream kinases into CSB kinase activity.

Summary: Human CSB associates with p53, allowing a specific binding refinement.

Reason: The verified PMID:7663514 abstract explicitly reports p53–CSB binding, but its original body remains unavailable. Independent PMID:22032989 Results/Figures4–5 use reciprocal/sequential human-cell immunoprecipitation and distinguish full-length CSB from CSB–PGBD3 in p53-containing assemblies. This supports specific p53 binding without claiming a purified binary affinity assay from the independent paper or assigning Mdm2 E3 catalysis to CSB.

Proposed replacements: p53 binding

Summary: The human CSB–CSA interaction is independently established.

Reason: PMID:7664335 remains abstract-only in this review. Independently read PMID:32355176 Figures2–3 identify the human CSB CSA-interacting motif and show motif-dependent CSA recruitment; PMID:34526721 supplies biochemical/structural evidence for the shared complex. The imported CSA partner is supported, while the old paper’s exact assay remains unverified. Keep this binding context as non-core; the stronger recruitment function is separately reviewed.

Summary: A human CSB fragment interacts with XPA in the source assay.

Reason: PMID:8999876 Results/Table1 and interaction Methods test the human CSB 528–1222 fragment against repair/transcription factors and support XPA association. Preserve the fragment scope rather than presenting every source interaction as full-length-protein reconstitution. Retain this supported generic binding as non-core.

Summary: A human CSB fragment interacts with the TFIIE p34 subunit.

Reason: PMID:8999876 Results/Table1 and interaction Methods support binding of human CSB residues528–1222 to TFIIE p34, the imported P29084 partner. This does not make CSB a constituent of TFIIE or transfer another factor’s activity. Keep the supported interaction as non-core.

Summary: ATP binding is directly measured independently of hydrolysis.

Reason: PMID:12560492 Table2 and Methods use ATPgammaS binding with purified human CSB; ATPase-defective E646Q retains nucleotide binding. Accept this ligand-binding activity separately from ATP hydrolysis and DNA movement.

Summary: Independent purified-human-CSB measurements establish ATP binding.

Reason: PMID:16107709 Table1 summarizes prior ATP-binding measurements rather than supplying a new binding assay for every mutant. The exact property is directly measured in PMID:12560492 Table2, including hydrolysis-defective but binding-competent E646Q. Accept ATP binding with this explicit independent support.

Summary: ATP binding is experimentally established for canonical CSB.

Reason: The current human record matches InterPro IPR000330 (SNF2 N-terminal domain). PMID:12560492, Materials and Methods (CSB protein purification, ATPase and ATP-binding assays) and Results/Figures 2–5, tests HA/His-tagged CSB expressed in insect cells: DNA stimulates ATP hydrolysis measured by TLC, while ATPγS filter binding directly measures nucleotide binding. Motif substitutions distinguish binding from hydrolysis; these data do not establish a helicase unwinding activity or activity of the CSB–PGBD3 fusion.

Summary: Canonical CSB nuclear localization can be refined to its independently demonstrated nucleoplasmic pool.

Reason: The actual PTHR45629 tree places human leaf PTN002473896 below the Eukaryota assertion node PTN001326493. The ungapped target MSA is an exact 1,493-residue match to Q03468, all three assigned IBD terms occur at that node, and no NOT is present on the target path. The nonhuman donor Q57UN8 is Tb927.7.4080: PMID:28727848 Methods nuclear purification/mass spectrometry and S1 Table, sheet S1B row 576, identify it in the procyclic T. brucei nuclear proteome (five peptides in S1A row 642; NES 2.306, p = 0.01793, with whole-cell missing values imputed). This is proteomic enrichment, not one of the six imaged fusion proteins. Independently, PMID:12560492 Methods Localization of ECFP-tagged CSB and Results/Figure 6 show functional CSB-ECFP predominantly in human fibroblast nuclei. The target in its own WITH/FROM is legitimate experimental grounding, not circularity. Neither experiment transfers canonical-CSB localization or function automatically to the fusion. Independently read human CSB imaging in PMID:16107709 Figures 4 and 5D resolves diffuse nucleoplasmic localization; PMID:12560492 supplies functional tagged-CSB corroboration. This added precision does not invalidate the original nuclear location or its verified source chain. The integrated review consistently refines the five broad canonical-CSB nucleus assertions to the independently observed nucleoplasmic pool. Conditional localization is retained in separate nucleolar annotations; the refinement does not imply exclusive localization or identify a nuclear-body class.

Proposed replacements: nucleoplasm

Summary: Human CSB occupies the nucleoplasm.

Reason: PMID:12560492 Results/fluorescence experiments show human CSB-ECFP distributed throughout the nucleus, with brighter foci in a subset of cells. Independent PMID:16107709 Figure 4/5 documents diffuse nucleoplasmic CSB. Refine the broad nucleus annotation to nucleoplasm without converting unspecified foci into a defined nuclear body. The integrated review consistently refines the five broad canonical-CSB nucleus assertions to the independently observed nucleoplasmic pool. Conditional localization is retained in separate nucleolar annotations; the refinement does not imply exclusive localization or identify a nuclear-body class.

Proposed replacements: nucleoplasm

Summary: Nucleoplasm is supported in addition to condition-dependent nucleolar CSB.

Reason: PMID:17626041 human-cell CSB-ECFP imaging describes nuclear distribution and oxidative-stress-associated nucleolar localization. Independent PMID:16107709 Figure 4/5 and PMID:12560492 resolve the diffuse nucleoplasmic pool. Refine this broad nucleus row while retaining the separate nucleolar assertion and its condition dependence. The integrated review consistently refines the five broad canonical-CSB nucleus assertions to the independently observed nucleoplasmic pool. Conditional localization is retained in separate nucleolar annotations; the refinement does not imply exclusive localization or identify a nuclear-body class.

Proposed replacements: nucleoplasm

Summary: The broad nuclear location can be refined to nucleoplasm.

Reason: PMID:32355176 studies human nuclear/chromatin transcription-repair assemblies. Independent human imaging in PMID:12560492 and PMID:16107709 establishes a diffuse nucleoplasmic CSB pool, supporting this more informative location. This does not identify every nuclear focus or imply exclusive localization. The integrated review consistently refines the five broad canonical-CSB nucleus assertions to the independently observed nucleoplasmic pool. Conditional localization is retained in separate nucleolar annotations; the refinement does not imply exclusive localization or identify a nuclear-body class.

Proposed replacements: nucleoplasm

Summary: Canonical CSB nuclear localization can be refined to its independently demonstrated nucleoplasmic pool.

Reason: The SL-0191 mapping describes the nucleus. PMID:12560492, Methods Localization of ECFP-tagged CSB and Results/Figure 6, shows wild-type CSB-ECFP in nuclei of human CS1AN.S3.G2 cells, in contrast to the distributed ECFP-only control; the tagged wild-type construct also rescues UV sensitivity. This supports nuclear localization of canonical CSB without relying on the HPA071297 antibody, whose antigen instead matches the fusion/PGBD3 sequence. Independently read human CSB imaging in PMID:16107709 Figures 4 and 5D resolves diffuse nucleoplasmic localization; PMID:12560492 supplies functional tagged-CSB corroboration. This added precision does not invalidate the original nuclear location or its verified source chain. The integrated review consistently refines the five broad canonical-CSB nucleus assertions to the independently observed nucleoplasmic pool. Conditional localization is retained in separate nucleolar annotations; the refinement does not imply exclusive localization or identify a nuclear-body class.

Proposed replacements: nucleoplasm

Summary: Nucleoplasmic CSB is supported independently of the product-ambiguous HPA reagent.

Reason: The HPA ERCC6 page reports nucleoplasm and nuclear bodies with HPA071297, but its 141-residue antigen is an exact match to P0DP91 residues 472–612 and standalone PGBD3 Q8N328 residues 4–144, and is absent from Q03468. Therefore the HPA image alone is not canonical-CSB-specific evidence. Independently, PMID:12560492 Methods and Results/Figure 6 report predominantly homogeneous nuclear distribution of functional CSB-ECFP, and the current human Reactome R-HSA-6781840 input is Q03468 residues 1–1493 in nucleoplasm. Retain the general localization with that independent support; the product assignment issue remains explicit.

Summary: Human CSB has a directly observed nucleoplasmic pool.

Reason: PMID:16107709 Methods and Figure4/5D examine endogenous human CSB in HeLa cells and report diffuse nucleoplasmic distribution before peroxide-induced redistribution. Accept the location; oxidative-stress foci are not automatically a distinct nuclear-body class.

Summary: CSB is an explicit nucleoplasmic participant in B-WICH recruitment of histone acetyltransferases.

Reason: The current official Reactome record R-HSA-5250930 (B-WICH recruits histone acetyltransferases) has an explicit forward participant chain 5250930 → 5250923 → 5250626 → 5365864 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in B-WICH recruitment of histone acetyltransferases, not evidence that CSB catalyzes every neighboring reaction.

Summary: CSB is an explicit nucleoplasmic participant in the B-WICH-associated histone acetylation complex.

Reason: The current official Reactome record R-HSA-5250938 (B-WICH:histone acetyltransferase acetylates histone H3 at lysine-9) has an explicit forward participant chain 5250938 → 5250927 → 5250942 → 5250923 → 5250626 → 5365864 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in the B-WICH-associated histone acetylation complex, not evidence that CSB catalyzes every neighboring reaction. The acetyltransferases in this assembly supply acetyl-transfer chemistry; CSB is a B-WICH component.

Summary: CSB is an explicit nucleoplasmic participant in B-WICH binding to the rDNA promoter.

Reason: The current official Reactome record R-HSA-5250947 (B-WICH complex binds rDNA promoter) has an explicit forward participant chain 5250947 → 5365864 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in B-WICH binding to the rDNA promoter, not evidence that CSB catalyzes every neighboring reaction.

Summary: CSB is an explicit nucleoplasmic participant in CSA recruitment to stalled RNA polymerase II.

Reason: The current official Reactome record R-HSA-6781833 (ERCC8 (CSA) binds stalled RNA Pol II) has an explicit forward participant chain 6781833 → 6781837 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in CSA recruitment to stalled RNA polymerase II, not evidence that CSB catalyzes every neighboring reaction.

Summary: CSB is an explicit nucleoplasmic participant in CSB binding to stalled RNA polymerase II.

Reason: The current official Reactome record R-HSA-6781840 (ERCC6 binds stalled RNA Pol II) has an explicit forward participant chain 6781840 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in CSB binding to stalled RNA polymerase II, not evidence that CSB catalyzes every neighboring reaction.

Summary: CSB is an explicit nucleoplasmic participant in CSB and polymerase ubiquitination.

Reason: The current official Reactome record R-HSA-6781867 (ERCC8:DDB1:CUL4:RBX1 ubiquitinates ERCC6 and RNA Pol II) has an explicit forward participant chain 6781867 → 6781839 → 6781837 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in CSB and polymerase ubiquitination, not evidence that CSB catalyzes every neighboring reaction. CSB is a ubiquitination target here; the location assertion does not assign ubiquitin-ligase activity to CSB.

Summary: CSB is an explicit nucleoplasmic participant in assembly of the ubiquitinated pre-incision complex.

Reason: The current official Reactome record R-HSA-6782004 (Assembly of the pre-incision complex in TC-NER) has an explicit forward participant chain 6782004 → 6781866 → 6781848 → 6781849 → 6781853, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in assembly of the ubiquitinated pre-incision complex, not evidence that CSB catalyzes every neighboring reaction. The terminal entity is ubiquitinated CSB (6781853), not a different natural product.

Summary: CSB is an explicit nucleoplasmic participant in USP7-mediated CSB deubiquitination.

Reason: The current official Reactome record R-HSA-6782069 (UVSSA:USP7 deubiquitinates ERCC6) has an explicit forward participant chain 6782069 → 6782066 → 6782068 → 6782065 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in USP7-mediated CSB deubiquitination, not evidence that CSB catalyzes every neighboring reaction. USP7 performs deubiquitination; CSB is its substrate in this event.

Summary: CSB is an explicit nucleoplasmic participant in the pre-incision complex during polymerase backtracking.

Reason: The current official Reactome record R-HSA-6782131 (ERCC2-facilitated RNA Pol II backtracking in TC-NER) has an explicit forward participant chain 6782131 → 6782066 → 6782068 → 6782065 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in the pre-incision complex during polymerase backtracking, not evidence that CSB catalyzes every neighboring reaction. The event’s discussion of TFIIH motor/helicase activities is not attributed to CSB by this location decision.

Summary: CSB is an explicit nucleoplasmic participant in recruitment of XPG and RPA.

Reason: The current official Reactome record R-HSA-6782138 (ERCC5 and RPA bind TC-NER site) has an explicit forward participant chain 6782138 → 6782111 → 6782122 → 6782112 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in recruitment of XPG and RPA, not evidence that CSB catalyzes every neighboring reaction.

Summary: CSB is an explicit nucleoplasmic participant in loading of ERCC1–XPF.

Reason: The current official Reactome record R-HSA-6782141 (Binding of ERCC1:ERCC4 (ERCC1:XPF) to pre-incision complex in TC-NER) has an explicit forward participant chain 6782141 → 6782134 → 6782111 → 6782122 → 6782112 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in loading of ERCC1–XPF, not evidence that CSB catalyzes every neighboring reaction.

Summary: CSB is an explicit nucleoplasmic participant in the complex after 5′ incision.

Reason: The current official Reactome record R-HSA-6782204 (5' incision of damaged DNA strand by ERCC1:ERCC4 in TC-NER) has an explicit forward participant chain 6782204 → 6782205 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in the complex after 5′ incision, not evidence that CSB catalyzes every neighboring reaction. Incision, DNA synthesis and ligation are performed by the corresponding nuclease, polymerase and ligase components.

Summary: CSB is an explicit nucleoplasmic participant in the post-incision DNA-synthesis complex.

Reason: The current official Reactome record R-HSA-6782208 (Repair DNA synthesis of ~27-30 bases long patch by POLD, POLE or POLK in TC-NER) has an explicit forward participant chain 6782208 → 6782222 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in the post-incision DNA-synthesis complex, not evidence that CSB catalyzes every neighboring reaction. Incision, DNA synthesis and ligation are performed by the corresponding nuclease, polymerase and ligase components.

Summary: CSB is an explicit nucleoplasmic participant in polymerase loading.

Reason: The current official Reactome record R-HSA-6782211 (DNA polymerases delta, epsilon or kappa bind the TC-NER site) has an explicit forward participant chain 6782211 → 6782205 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in polymerase loading, not evidence that CSB catalyzes every neighboring reaction. Incision, DNA synthesis and ligation are performed by the corresponding nuclease, polymerase and ligase components.

Summary: CSB is an explicit nucleoplasmic participant in the complex undergoing XPG 3′ incision.

Reason: The current official Reactome record R-HSA-6782224 (3' incision by ERCC5 (XPG) in TC-NER) has an explicit forward participant chain 6782224 → 6782219 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in the complex undergoing XPG 3′ incision, not evidence that CSB catalyzes every neighboring reaction. Incision, DNA synthesis and ligation are performed by the corresponding nuclease, polymerase and ligase components.

Summary: CSB is an explicit nucleoplasmic participant in repair-patch ligation.

Reason: The current official Reactome record R-HSA-6782227 (Ligation of newly synthesized repair patch to incised DNA in TC-NER) has an explicit forward participant chain 6782227 → 6782220 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in repair-patch ligation, not evidence that CSB catalyzes every neighboring reaction. Incision, DNA synthesis and ligation are performed by the corresponding nuclease, polymerase and ligase components.

Summary: CSB is an explicit nucleoplasmic participant in recovery of RNA synthesis.

Reason: The current official Reactome record R-HSA-6782234 (Recovery of RNA synthesis after TC-NER) has an explicit forward participant chain 6782234 → 6782230 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in recovery of RNA synthesis, not evidence that CSB catalyzes every neighboring reaction.

Summary: CSB is an explicit nucleoplasmic participant in the partially opened pre-incision complex.

Reason: The current official Reactome record R-HSA-9684118 (ERCC3-facilitated RNA Pol II backtracking in TC-NER) has an explicit forward participant chain 9684118 → 9684117 → 9684121 → 9684120 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in the partially opened pre-incision complex, not evidence that CSB catalyzes every neighboring reaction. The event’s discussion of TFIIH motor/helicase activities is not attributed to CSB by this location decision.

Summary: CSB is an explicit nucleoplasmic participant in the mixed-species rDNA-associated methyltransferase complex.

Reason: The current official Reactome record R-NUL-573373 (Ttf-I:rRNA Promoter:Ercc6:Ehmt2 complex dimethylates histone H3 at lysine-9) has an explicit forward participant chain 573373 → 573387 → 573330 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in the mixed-species rDNA-associated methyltransferase complex, not evidence that CSB catalyzes every neighboring reaction. The R-NUL record and complex 573330 are explicitly chimeric: the model mixes human CSB with mouse components, so it is not a wholly human reconstituted experiment. The actual target component remains human Q03468; G9a methyltransferase and CHD4 remodeling activities are not transferred to CSB. General human nuclear localization is independently supported by PMID:12560492.

Summary: CSB is an explicit nucleoplasmic participant in recruitment of the mixed-species rDNA-associated complex.

Reason: The current official Reactome record R-NUL-573385 (Recruitment of CSB, G9a, and NuRD to the rRNA promoter) has an explicit forward participant chain 573385 → 54429, ending at human Q03468 residues 1–1493 in GO:0005654 nucleoplasm. This is evidence of CSB localization in recruitment of the mixed-species rDNA-associated complex, not evidence that CSB catalyzes every neighboring reaction. The R-NUL record and complex 573330 are explicitly chimeric: the model mixes human CSB with mouse components, so it is not a wholly human reconstituted experiment. The actual target component remains human Q03468; G9a methyltransferase and CHD4 remodeling activities are not transferred to CSB. General human nuclear localization is independently supported by PMID:12560492.

Summary: The source experiment specifically resolves chromatin association.

Reason: PMID:26620705 fractionation Methods and Figure4C recover SUMO-associated human CSB in the chromatin fraction. Chromatin is the directly established subcomponent of the broader chromosome term, so refine accordingly; no individual chromosome or centromeric localization is inferred.

Proposed replacements: chromatin

Summary: Human CSB acts in a chromatin-associated transcription-repair assembly.

Reason: PMID:32355176 uses solubilized chromatin, endogenous RNAPII co-IP and human CSB recruitment/rescue experiments. This directly supports chromatin rather than a less informative whole-chromosome assignment. The refinement does not imply constitutive association with all chromosomes.

Proposed replacements: chromatin

Summary: Chromatin is the more precise location for the demonstrated chromosome-associated CSB pool.

Reason: GO:0000785 chromatin denotes the organized DNA–protein complex forming chromosomes. The broad SL-0468 chromosome mapping can be refined to that material: PMID:29203878, Results CSB evicts histones from chromatin flanking DNA DSBs in vivo and Figure 5, places the CSB-dependent remodeling response around an I-PpoI break on human chromosome 1; the tagged-CSB recruitment assays and chromatin methods distinguish this from a generic chromosome structural component. Wild-type CSB rescues histone displacement whereas ATPase-dead W851R does not. This is a cellular chromatin context, not evidence for constitutive coating of every chromosome or a fusion-product assignment.

Proposed replacements: chromatin

Summary: A contextual human nucleolar CSB pool is supported independently.

Reason: The operative PMID:16107709 sections establish nucleoplasm/oxidative redistribution but did not resolve the nucleolus claim directly. PMID:17626041 human CSB-ECFP imaging provides positive nucleolar evidence under oxidative stress; PMID:31970402 establishes a human rDNA/PolI regulatory context. Retain nucleolus as a supported non-core location with these source limits.

Summary: Human CSB can localize to nucleoli under oxidative stress.

Reason: PMID:17626041 Methods and Figures5–6 distinguish human CS1AN cells complemented with CSB-ECFP from separate mouse ABL experiments. The human imaging supports nuclear/nucleolar redistribution after peroxide. Keep this conditional nucleolar location as non-core rather than assuming constitutive nucleolar residence.

Summary: Independent human experiments support the nucleolar context.

Reason: PMID:23555303 operative experiments concern NM1/WSTF/SNF2h and do not isolate CSB localization. Independently read PMID:17626041 human CSB-ECFP imaging provides nucleolar evidence and PMID:31970402 examines human CSB-dependent rDNA transcription. Keep this location as non-core, retaining the NAS source and its assay limitation.

Summary: The broad electronic DNA-repair prediction is supported by target-specific repair biochemistry and cellular evidence.

Reason: The current ARBA00029008 rule contains a matching FunFam condition 3.40.50.300:FF:000863, present on actual human Q03468; rule membership is provenance, not an independent experiment. Human CSB is explicitly recruited to stalled polymerase in Reactome R-HSA-6781840, and PMID:29203878 Results/Figure 5 demonstrates ATPase-dependent chromatin remodeling at induced DNA breaks. These establish an active repair-associated role rather than a disease association alone. Broad DNA repair is retained because the evidence spans transcription-coupled repair and a double-strand-break chromatin role; the fusion is not assumed equivalent.

Summary: The inherited transcription-coupled repair function agrees with direct target evidence and the human pathway.

Reason: The actual PTHR45629 tree places human leaf PTN002473896 below the Eukaryota assertion node PTN001326493. The ungapped target MSA is an exact 1,493-residue match to Q03468, all three assigned IBD terms occur at that node, and no NOT is present on the target path. The target’s own experimental grounding is valid and the multi-species WITH/FROM is not a pairwise similarity vote. Reactome R-HSA-6781840 identifies canonical human CSB binding damage-stalled polymerase, and its downstream pre-incision complexes contain the same Q03468 protein. The actual rat donor original PMID:31644904, Results Rats exhibit repair deficiency, Figure 2 and STAR Methods, independently shows impaired post-UV RNA-synthesis recovery with preserved unscheduled DNA synthesis in R571X fibroblasts. These observations support conserved transcription-coupled repair without making CSB the lesion-incising nuclease.

Summary: Human CSB recruits and organizes the transcription-coupled repair assembly.

Reason: PMID:32355176 human U2OS knockout/rescue, endogenous stalled-RNAPII co-IP and CSB-CIM experiments establish CSB-dependent CSA/UVSSA/TFIIH assembly after UV. This is a mechanistic contribution to transcription-coupled nucleotide-excision repair, not mere sensitivity or complex membership. Xenopus NPE/CRL4 assays are kept distinct from the human recruitment evidence.

Summary: CSB supplies ATP-dependent mechanical and assembly functions in transcription-coupled repair.

Reason: PMID:34526721 Results/Figures1–4 and Methods examine recombinant human CSB with mammalian PolII and repair factors. ATPase K538R and pulling-hook F796 perturbations distinguish ATP-dependent arrest passage, while structures position CSB on upstream DNA with CSA/UVSSA. Pig PolII and mouse RBX1 components are explicitly distinct from the human CSB protein; static structures are not real-time stepping measurements.

Summary: CSB contributes directly to the mammalian transcription-repair assembly.

Reason: PMID:38316879 main Results/Figures1–3 and Methods examine human CSB with mammalian PolII and ELOF1/repair factors. The biochemical/structural assembly supports CSB’s established transcription-coupled repair role. Do not transfer ELOF1-specific positioning or ubiquitination effects as an intrinsic CSB enzyme activity; the PolII preparation is pig.

Summary: Human CSB supports transcription-coupled repair in the source’s UV controls.

Reason: PMID:38600235 human HAP1/RPE1 knockout and wild-type/K538R rescue experiments include UV RNA-recovery and illudin controls (Figures1/5), supporting the established TC-NER contribution. The paper also studies DNA–protein-crosslink repair, which is not treated as nucleotide-excision repair merely because CSB participates in both.

Summary: Human CSB restores recovery after transcription-blocking UV damage.

Reason: PMID:9565609 original Methods/Results and Figures2–5/TableII were independently read in the linked source guide. Microinjected purified full-length human CSB restores post-UV RNA synthesis in CS1AN fibroblasts, with specificity controls and partial K538R rescue. The endpoint is RNA recovery, not isolated lesion-excision kinetics; independent PMID:32355176 supplies the recruitment mechanism underlying the established TC-NER role.

Summary: The rat-orthology transfer of transcription-coupled repair is well grounded.

Reason: The actual current rat donor A0A0G2JTU1/ENSRNOP00000068845 has IMP support from PMID:31644904. Its original Results repair-deficiency section, Figure 2 and STAR Methods compare primary skin fibroblasts from homozygous R571X rats with heterozygous littermates. The mutation models human R652X; this is a rat perturbation experiment, not a human construct assay. After UV, mutant cells fail to restore nascent RNA synthesis and retain CPD staining, while the EdU unscheduled-DNA-synthesis assay remains comparable to controls. The latter separates the defect from a general loss of global-genome NER. Human CSB’s explicit binding to stalled polymerase and presence in the downstream Reactome TCR complexes provide target corroboration. The transfer does not extend automatically to CSB–PGBD3.

Summary: Human CSB supports repair of transcription-blocking CPDs.

Reason: PMID:10564257 Methods, Results and Table1 use human wild-type CSB or E646Q cDNA in hamster UV61 cells and measure repair at the active DHFR gene with T4 endonuclease V/Southern analysis. Wild-type human CSB restores the repair phenotype whereas E646Q does not. The host is hamster but the complemented protein is human CSB; no fusion equivalence is inferred.

Summary: Human CSB function and its SUMO regulation contribute to UV transcription recovery.

Reason: PMID:26620705 Methods and Figures4/7 show wild-type CSB rescue of UV RNA recovery in human cells and impaired responses with relevant CSB variants/SUMO perturbation. This supports the established TC-NER role with the RNA-recovery endpoint stated; chromatin fractionation is a separate supporting observation.

Summary: The source establishes altered BER capacity but leaves CSB’s own BER participation unresolved.

Reason: PMID:9973627 Methods/Results and Figures1–4 show restoration of OGG1 mRNA and whole-extract 8-oxoguanine incision after CSB complementation in human fibroblasts. The current GO:0006284 definition describes glycosylase removal, sugar-phosphate excision and gap filling/ligation. These experiments can be explained by regulation of OGG1/repair capacity and do not identify which BER step CSB itself performs or scaffolds. Retain uncertainty rather than claiming CSB catalysis or treating this positive cellular phenotype as false.

Summary: Human CSB has independently verified chromatin-remodeling activity.

Reason: PMID:12769854 remains original-inaccessible; its abstract focus on BRG1/SNF2h does not establish a wrong-gene citation. Independently read PMID:29203878 Figure5 shows CSB-dependent loss of H2A/H2B around a human I-PpoI break, rescued by wild-type but not ATPase-defective CSB. This establishes the biological chromatin-remodeling assertion while preserving the old NAS source’s access limit.

Summary: CSB directly contributes to transcription by RNA polymerase II.

Reason: PMID:7664335 remains abstract-only. Independent PMID:9326587 directly reconstitutes stimulation of human RNAPII elongation by human CSB, with CSB immunodepletion controls and polymerase interaction, and PMID:24874740 provides human-cell recruitment/transcription evidence. Accept the broad process because CSB does functional work in transcription, while not claiming that the inaccessible old paper’s exact experiment was verified.

Summary: CSB participates in the cellular oxidative-stress response with PARP1.

Reason: PMID:16107709 Methods/Results establish human CSB–PARP1 interaction, peroxide-dependent redistribution and functional perturbation responses. These support a contextual stress-response role. They do not establish that CSB prevents DNA oxidation, activates PARP1, or directly catalyzes base removal.

Summary: CSB regulates the ABL-associated oxidative-stress response.

Reason: PMID:17626041 human-cell rescue and ABL-associated kinase assays, alongside separately identified mouse experiments, support CSB-dependent responses to peroxide. Retain the contextual regulatory process; CSB is not the tyrosine kinase and the evidence is not generalized to every oxidative lesion.

Summary: CSB forms a functional association with the transcription elongation machinery.

Reason: PMID:9326587 actual Methods/Results use human CSB and human RNAPII in elongation reactions and interaction experiments; CSB increases elongation and immunodepletion removes the stimulation. This fits the current elongation-factor-complex definition, which encompasses complexes interacting with PolII to alter elongation. It does not assert TFIIH membership or an invariant complex stoichiometry.

Summary: The broad ATP-dependent DNA activity can be refined to DNA translocation.

Reason: PMID:12560492 separately measures human CSB ATP binding, hydrolysis and duplex binding. Independent PMID:34526721 structure/functional analysis supports ATP-driven movement on upstream DNA in the PolII complex, including K538R and F796 perturbations. Refine the broad activity to DNA translocase; the original ATPase assay alone is not relabeled as a direct stepping assay.

Proposed replacements: DNA translocase activity

Summary: DNA translocation is the supported specific motor function.

Reason: PMID:16107709 measures regulation of human CSB ATPase by PARP1 modification. Independent PMID:34526721 establishes the ATP-dependent DNA motor mechanism in the PolII complex, supporting refinement from the broad ATP-dependent DNA activity. ATP binding and hydrolysis remain separately reviewed; this is not helicase strand unwinding.

Proposed replacements: DNA translocase activity

Summary: The motor is better represented by DNA translocase activity.

Reason: PMID:8999876 establishes human CSB DNA-stimulated ATPase, duplex binding and negative helicase results. Independent PMID:34526721 supplies the biochemical/structural basis for ATP-driven movement on upstream DNA during PolII arrest passage. Refine the broad motor term without claiming that the 1997 experiment measured translocation directly.

Proposed replacements: DNA translocase activity

Summary: Human CSB’s ATP-dependent DNA motor can be specified as a translocase.

Reason: PMID:25820262 compares human CSB knockout and wild-type/ATPase-defective rescue in DNA-damage responses; these cellular assays establish ATPase dependence but not isolated movement. Independently read PMID:34526721 supplies the translocation mechanism and motor perturbations. Refine the broad term using this combined evidence, preserving the assay distinction.

Proposed replacements: DNA translocase activity

Summary: Canonical-CSB nuclear-body localization remains unresolved by the HPA evidence.

Reason: The current HPA071297 image and cell-line records do show nuclear puncta, but the full 141-residue immunogen is absent from canonical Q03468 and exactly shared by CSB–PGBD3 and standalone PGBD3. HPA’s predicted target size is 119.5 kDa and its western assessment notes additional bands. These facts prevent a uniquely canonical-CSB assignment; they are not a measured cross-reactivity experiment. PMID:12560492 Results/Figure 6 describes brighter CSB-ECFP foci in about 20% of cells, but neither their identity as a GO:0016604 membraneless nuclear body nor equivalence to the HPA puncta is established in the inspected text. Retain uncertainty for this precise compartment without denying CSB nuclear localization.

Summary: Human CSB directly hydrolyzes ATP in the XPG/DNA-bubble experiments.

Reason: PMID:16246722 Methods and Figure4 quantify phosphate release from gamma-32P ATP by purified full-length human CSB, with XPG and DNA substrate controls. Hydrolysis is directly measured, and XPG preferentially stimulates it on a bubble substrate. Preserve this catalytic activity independently of translocation or helicase terminology.

Summary: Purified full-length human CSB catalyzes ATP hydrolysis.

Reason: PMID:9565609 actual Methods/Results and TableII directly compare wild-type and K538R human CSB purified from Sf21 cells. DNA strongly stimulates hydrolysis; secondary structure affects apparently single-stranded DNA stimulation. Accept ATP hydrolysis as measured chemistry, separately from ATP binding and chromatin remodeling.

Summary: The Rhea ATP-hydrolysis mapping matches experimentally observed CSB chemistry.

Reason: The actual RHEA:13065 equation is ATP + water → ADP + phosphate + proton. PMID:12560492, Materials and Methods (CSB protein purification, ATPase and ATP-binding assays) and Results/Figures 2–5, tests HA/His-tagged CSB expressed in insect cells: DNA stimulates ATP hydrolysis measured by TLC, while ATPγS filter binding directly measures nucleotide binding. Motif substitutions distinguish binding from hydrolysis; these data do not establish a helicase unwinding activity or activity of the CSB–PGBD3 fusion. The hydrolysis is the biochemical energy source for CSB motor/remodeling functions; its positive assay is not evidence that the natural fusion retains the ATPase domain.

Summary: Human CSB contributes to the tested neuronal-development program.

Reason: PMID:24874740 uses CSB knockdown in human ReNcell VM cells, neuronal marker/neurite readouts and transcriptional recruitment experiments. This supports contextual neurogenesis participation through gene regulation. Keep it as non-core without treating the developmental phenotype as a distinct CSB catalytic activity or generalizing to every neural lineage.

Summary: CSB supports neuronal differentiation in the human-cell model.

Reason: PMID:24874740 Results/Figures1–8 show impaired neuronal differentiation after human CSB depletion, accompanied by altered promoter occupancy/BAF and PolII recruitment. These are positive context-specific data, so retain non-core participation rather than rejecting the term solely because the mechanism is regulatory.

Summary: CSB positively regulates ABL tyrosine-kinase activity in the tested context.

Reason: PMID:17626041 human CSB-complemented cells and ABL-associated GST-Crk phosphorylation assays show oxidative-stress-dependent kinase activation associated with functional CSB; direct CSB–ABL interaction is separately demonstrated. Retain the activator function as non-core, with cellular/immunopurified-complex attribution limits rather than describing CSB as a kinase or a fully reconstituted two-protein activation system.

Summary: CSB supports neurite development in the tested human neural cells.

Reason: PMID:24874740 human ReNcell VM CSB knockdown reduces neurite/projection development together with neuronal transcriptional recruitment. This supports the existing process as a contextual, non-core regulatory contribution; it does not imply that CSB is a structural component of the projection.

Summary: The measured effect is positive regulation of RNA polymerase II elongation.

Reason: PMID:9326587 actual Methods/Results and Figure 1 display stimulation of human RNAPII elongation after a 112-nucleotide U-less cassette by human CSB; CSB immunodepletion removes stimulation. A separate promoter-independent-template result is reported as data not shown, and is not described here as a displayed or independently inspected experiment. Refine the broader elongation-regulation term to the current PolII-specific positive regulation term. The reconstitution uses human CSB/PolII and general factors, with yeast TBP separately identified; it is not evidence for positive elongation of every RNA polymerase.

Proposed replacements: positive regulation of transcription elongation by RNA polymerase II

Summary: The measured effect is positive regulation of RNA polymerase II elongation.

Reason: PMID:9326587 actual Methods/Results and Figure 1 display stimulation of human RNAPII elongation after a 112-nucleotide U-less cassette by human CSB; CSB immunodepletion removes stimulation. A separate promoter-independent-template result is reported as data not shown, and is not described here as a displayed or independently inspected experiment. Refine the broader elongation-regulation term to the current PolII-specific positive regulation term. The reconstitution uses human CSB/PolII and general factors, with yeast TBP separately identified; it is not evidence for positive elongation of every RNA polymerase.

Proposed replacements: positive regulation of transcription elongation by RNA polymerase II

Summary: Human CSB directly promotes RNA polymerase II elongation.

Reason: The actual current rat donor A0A0G2JTU1/ENSRNOP00000068845 has IMP support from PMID:31644904. Its original Results repair-deficiency section, Figure 2 and STAR Methods compare primary skin fibroblasts from homozygous R571X rats with heterozygous littermates. The mutation models human R652X; this is a rat perturbation experiment, not a human construct assay. Figure 2C and the main Results report impaired post-UV transcription recovery and a supplementary qRT-PCR elongation endpoint; the detailed supplementary panel was not inspected. Independently, actual human PMID:9326587 Materials and Methods, Results CSB Stimulates Transcriptional Elongation and Figure1 show purified CSB stimulating elongation after a 112-nucleotide U-less cassette, with loss of stimulation upon CSB immunodepletion. A promoterless-template result is reported as data not shown. The reconstitution uses human RNA polymerase II and general factors, plus yeast TBP; the separate binding assay uses a CSB 528–1222 MBP fragment. The direct elongation experiment establishes active regulation beyond the rat recovery phenotype, supporting positive regulation of RNA polymerase II elongation. GO:0032968 captures both the positive direction and the measured polymerase specificity, refining the imported broad regulatory process without assigning polymerase catalysis to CSB.

Proposed replacements: positive regulation of transcription elongation by RNA polymerase II

Summary: The transferred DNA-protection assertion needs a more discriminating mechanistic basis.

Reason: The actual current rat donor A0A0G2JTU1/ENSRNOP00000068845 has IMP support from PMID:31644904. Its original Results repair-deficiency section, Figure 2 and STAR Methods compare primary skin fibroblasts from homozygous R571X rats with heterozygous littermates. The mutation models human R652X; this is a rat perturbation experiment, not a human construct assay. The relevant oxidative-stress result is hypersensitivity to potassium bromate (main Results, Figure S2C reference); STAR Methods Clonogenic survival assay treats cells for 3 h and measures surviving colonies after recovery. The inspected work establishes damage sensitivity and repair/transcription consequences, but this assay alone does not separate prevention of DNA damage (GO:0042262) from repair of existing damage or downstream survival. The detailed supplement was not independently inspected. Preserve the current donor provenance and leave the specific protection claim unresolved rather than asserting that CSB cannot protect DNA.

Summary: Full-length CSB positively influences repair with a distinguishable fusion contribution.

Reason: PMID:22483866 separates full-length human CSB and CSB–PGBD3 expression in UVSS1KO cells and measures UV RNA recovery and host-cell reactivation. The proteins have distinguishable and combined effects. Retain positive DNA-repair regulation as non-core, preserving the imported IGI/IMP context and partner identity rather than merging the fusion with the canonical ATPase or treating reporter recovery as identification of a new repair chemistry.

Summary: Full-length CSB positively influences repair with a distinguishable fusion contribution.

Reason: PMID:22483866 separates full-length human CSB and CSB–PGBD3 expression in UVSS1KO cells and measures UV RNA recovery and host-cell reactivation. The proteins have distinguishable and combined effects. Retain positive DNA-repair regulation as non-core, preserving the imported IGI/IMP context and partner identity rather than merging the fusion with the canonical ATPase or treating reporter recovery as identification of a new repair chemistry.

Summary: Independent human experiments establish positive regulation of PolI transcription by CSB.

Reason: PMID:23555303 primarily assays NM1/WSTF/SNF2h, not selective CSB function in the operative sections read. Independent PMID:31970402 Figures5–6 uses human CSB depletion and wild-type versus UBD-mutant rescue to link CSB to Nucleolin/PolI occupancy and pre-rRNA synthesis. This positively establishes the regulatory role, retained as non-core, without attributing RNA polymerization itself to CSB.

Summary: Human CSB positively regulates PolII transcription.

Reason: PMID:26044184 operative experiments focus on NM1 perturbation rather than selective CSB function. Independent PMID:9326587 directly shows human CSB stimulation of PolII elongation, and PMID:24874740 shows human-cell promoter/recruitment effects. Accept the biological assertion while preserving the original NAS source and its more indirect assay scope.

Summary: The source establishes a PolIII-associated complex but does not resolve CSB-specific positive regulation.

Reason: PMID:16603771 identifies CSB in the purified human B-WICH assembly. Its PolIII occupancy and transcription perturbations principally assay WSTF/SNF2h/NM1 and WSTF knockdown at 5S/7SL loci. Those experiments support the complex’s regulatory role, but the inspected operative text does not distinguish a necessary CSB contribution to that output. Keep this particular functional assertion unresolved; complex membership is retained separately and is not treated as false.

Summary: CSB recruits repair proteins to damaged transcription-associated chromatin.

Reason: PMID:32355176 Figures2–5 use human CSB CIM deletions, LacO tethering and knockout/rescue to establish CSA recruitment and downstream assembly at chromatin-associated stalled RNAPII. This is direct recruitment work, not merely correlated abundance, and supports protein localization to chromatin. Xenopus biochemical assays are not substituted for these human recruitment measurements.

Summary: CSB is recruited to DNA-damage sites in the human-cell experiments.

Reason: PMID:28292928 Figures1–3 and Methods measure CSB-dependent Elongin A/CUL5 assembly and localization at laser-induced damage in human U2OS/CS1AN cells. Accept the CSB location with the tagged-construct and induced-damage scope; the separately assayed Elongin A construct is rat.

Summary: Human CSB associates with UV-damaged transcription sites.

Reason: PMID:32355176 human UV-stalled RNAPII co-IP, chromatin isolation and rescue experiments establish recruitment of CSB to the relevant damage-associated transcription assembly. This supports the site-of-damage location without claiming autonomous affinity for a naked lesion or every type of DNA damage.

Summary: The positive repair evidence supports broader double-strand-break repair, without resolving classical end joining.

Reason: PMID:29545921 Figures3/5 directly monitor neutral-comet repair kinetics after MMS/IR in human CSB-deficient and complemented cells. G1 and 53BP1 observations are compatible with end joining, but the read assays do not isolate the KU/DNA-PK/XRCC4–LIG4 classical pathway required by GO:0097680. Refine to broader double-strand-break repair, also supported mechanistically by human CSB-dependent histone eviction at a break in PMID:29203878 Figure5. This preserves the positive evidence and leaves pathway-specific attribution open.

Proposed replacements: double-strand break repair

Summary: CSB is a biochemically identified component of the human B-WICH preparation.

Reason: PMID:16603771 purification Methods and Results/Figures2–3 identify CSB by mass spectrometry and immunoblotting in a large human HeLa nuclear WSTF/SNF2h-containing assembly. Retain this supported complex location as non-core. Membership alone does not establish that every WSTF-dependent PolIII output is specifically executed by CSB.

Summary: CSB supplies chromatin-associated recruitment/adaptor activity.

Reason: The current GO:0140463 definition concerns bringing protein and chromatin together to establish or maintain localization. PMID:32355176 human CIM deletion, LacO tethering and stalled-RNAPII recruitment/rescue experiments show CSB-dependent CSA recruitment and repair-complex assembly. These functional linkage experiments justify the adaptor assertion beyond generic co-IP alone.

Summary: ATP-dependent chromatin remodeling is a directly supported inherited CSB activity.

Reason: The actual PTHR45629 tree places human leaf PTN002473896 below the Eukaryota assertion node PTN001326493. The ungapped target MSA is an exact 1,493-residue match to Q03468, all three assigned IBD terms occur at that node, and no NOT is present on the target path. The sole extant donor listed for this IBD is the target itself, which is valid experimental grounding and not circularity. Independently inspected PMID:29203878, Results CSB evicts histones from chromatin flanking DNA DSBs in vivo, Figure 5c–f and ChIP/I-PpoI Methods, shows that loss of CSB prevents H2A/H2B displacement near a human chromosomal break; full-length Myc-CSB rescues while ATPase-dead W851R does not. This is direct cellular ATP-dependent remodeling support, not a claim that purified nucleosome sliding was inspected in that paper or that every chromatin association requires ATPase activity. The fusion lacks the canonical motor region and is not included by this ancestry proof.

Summary: Independent human experiments establish ATP-dependent chromatin remodeling by CSB.

Reason: PMID:9565609 shows nucleosomal-DNA-stimulated CSB ATPase, which by itself is not a remodeling assay. Independently read PMID:29203878 Figure5 compares human wild-type and ATPase-defective CSB rescue of H2A/H2B eviction around an I-PpoI break. That targeted chromatin readout supports the specific activity. Preserve the distinction between the original ATPase experiment and the independent remodeling evidence.

Summary: CSB ATPase function drives histone displacement at human DNA breaks.

Reason: PMID:29203878 Figure5 and associated Methods use human CSB knockout with wild-type versus W851R rescue and measure H2A/H2B occupancy around an I-PpoI break. The ATPase-dependent eviction supports chromatin-remodeler activity. This is a targeted cellular remodeling assay, not purified nucleosome sliding or proof of all remodeling modes.

Summary: CSB performs ATP-dependent damage sensing in the stalled-PolII repair system.

Reason: GO:0140664 covers recognition of toxic DNA structures and initiation of an ATP-driven signaling response. PMID:32355176 establishes human CSB recruitment to UV-stalled PolII and CIM-dependent assembly of CSA/UVSSA/TFIIH; independent PMID:34526721 resolves the upstream-DNA motor and ATPase-dependent PolII arrest-passage mechanism. The supported interpretation is that CSB acts within the PolII–DNA assembly: ATP-driven engagement with upstream DNA tests whether the transcriptional obstruction can be overcome and couples persistent arrest to repair-factor recruitment. This gives the damage-sensor annotation a polymerase-coupled mechanistic basis. It does not require autonomous affinity for an isolated lesion, assign direct base excision, or claim direct observation of every proposed ATP-cycle step.

Summary: Human CSB positively regulates homologous-recombination repair in the tested cells.

Reason: PMID:25820262 human-cell CSB perturbation/rescue and DR-GFP repair assays show a positive HR contribution, with ATPase-dependent chromatin effects providing a mechanistic context. Retain this supported regulatory process as non-core rather than assigning strand exchange or recombinase catalysis to CSB.

Summary: CSB shifts repair away from nonhomologous end joining in the tested reporter context.

Reason: PMID:25820262 uses human CSB knockout/rescue and end-joining/HR reporters to show increased NHEJ when CSB is lost. Retain negative regulation as a non-core pathway-choice contribution, with the reporter/cell-state scope explicit. This does not contradict a positive broader DSB-repair contribution in other settings or establish universal suppression of classical end joining.