CRX

Summary: CRX associates with regulatory chromatin.

Reason: The TFclass source is consistent with human CRX CUT&Tag occupancy in retinal organoids. The assay measures chromatin association; individual target reporter tests supply the separate transcriptional interpretation. The classification is not itself an imaging experiment.

Summary: The bovine CRX chromatin association is transferable.

Reason: The literal donor Q9XSK0 carries experimentally curated chromatin localization from PMID:18854042. Its retinal nuclear-complex experiments and the independent human CUT&Tag results support chromatin association, while bovine and mouse assay contexts remain distinct.

Summary: CRX recognizes RNA polymerase II regulatory DNA.

Reason: Current ARBA00028973 branch 12 matches the official FunFam 1.10.10.60:FF:000068 and Eukaryota lineage. The source also names mouse Crx and its Ensembl product. This broad regulatory-region assertion agrees with human competitive OTX-element EMSA and reporter tests; the matching rule is provenance, not a substitute for those assays.

Summary: The bovine regulatory-DNA binding assertion is supported.

Reason: Q9XSK0 has a current IDA annotation to this exact term from PMID:18854042. That study combines retinal nuclear extracts, CRX-responsive elements and cofactor experiments. Independent purified human CRX EMSA establishes sequence-selective regulatory DNA binding; no bovine promoter-occupancy result is mislabeled as a human assay.

Summary: Inherited cis-regulatory DNA binding is supported in CRX.

Reason: The exact 299-residue human sequence lies beneath PTN000677464 in the current PTHR45793 tree; the corresponding GO:0000978 IBD is present and no loss record lies on the target path. Human CRX OTX-element binding directly corroborates the conserved activity. Current-tree reconstruction is distinct from reconstructing the historical curator session, and legitimate human self-evidence is retained.

Summary: Human CRX binds specific cis-regulatory sequences.

Reason: PMID:10625658 tested bacterially produced GST-human CRX with OTX and PCE-1 probes and unrelated competition controls. OTX binding and OTX-dependent reporter activation establish the annotated sequence-specific interaction. The paper also studies RX; its separate tissue-localization and developmental experiments are not attributed to CRX.

Summary: CRX is an inherited RNA polymerase II DNA-binding transcription factor.

Reason: The current target path descends from the literal PTN000677464 GO:0000981 IBD, with no mapped loss along that path. Human sequence-specific DNA binding and transcriptional reporter assays support the activity. The integrated molecular function accommodates both measured activation and context-dependent repression; it is not inferred from donor number.

Summary: The Otx-family mapping agrees with direct CRX transcription-factor activity.

Reason: The official CRX record contains IPR017970 and the literal InterPro2GO mapping supports the activity. Human CRX DNA binding and reporter activation establish the same molecular role independently. Later human assays also show repression of selected targets, so an activator-only replacement would narrow the integrated activity unnecessarily.

Summary: The TFclass assignment correctly identifies a sequence-specific transcription factor.

Reason: The source class tfclass:3.1.3 is preserved as the classification premise. Direct human CRX EMSA and regulatory-element reporter experiments support the RNA polymerase II transcription-factor activity; no independent reconstruction of the TFclass database is claimed.

Summary: Specify the RNA polymerase II activator activity.

Reason: The literal bovine CRX donor has positive activation evidence from PMID:18854042. Human CRX independently activates OTX-containing promoters in PMID:10625658. GO:0001228 is the supported RNA polymerase II-specific child of this broad activator term. This precision change preserves the positive donor assertion; repression in other contexts does not negate these activation assays.

Proposed replacements: DNA-binding transcription activator activity, RNA polymerase II-specific

Summary: Human CRX activates RNA polymerase II promoter reporters.

Reason: Complete human CRX coding-sequence constructs increased normalized arrestin and IRBP promoter CAT activity, and OTX-containing heterologous reporters responded to CRX. These are positive activation assays even though CRX can repress other targets in other contexts.

Summary: The broad homeodomain DNA-binding mapping is correct.

Reason: The official record contains the mapped homeobox domain IPR001356. Purified human CRX binds regulatory DNA with sequence-specific competition controls. The broad electronic assertion is sound at its source precision; the existing specific DNA-binding rows retain the more detailed experimental coverage.

Summary: Mouse-to-human chromatin binding is supported.

Reason: The literal mouse donor O54751 carries IDA chromatin binding from PMID:14613968, whose complete abstract reports Crx and ataxin-7 occupancy at retinal promoters and enhancers. The original full Methods were not recovered here, but independent human CRX CUT&Tag supports the transferred activity. Chromatin association does not by itself assign ataxin-7 regulatory activity to CRX.

Summary: The combined electronic transcription-factor mapping is biologically sound.

Reason: ARBA00028295 branch 57 matches the current CRX FunFam; the original row also names O54751, its Ensembl product and IPR013851. Direct human DNA-binding and reporter experiments support the broad activity. Retain this correct broad source assertion while the experimental and refined ISS rows provide RNA polymerase II specificity.

Summary: Specify RNA polymerase II transcription-factor activity.

Reason: The mouse ortholog transfer is positive, and direct human CRX DNA-binding and reporter assays support GO:0000981. This is a target-supported specificity refinement of GO:0003700, not evidence that the donor annotation failed. Activation and context-dependent repression are both retained.

Proposed replacements: DNA-binding transcription factor activity, RNA polymerase II-specific

Summary: Specify the molecular activity established independently in human CRX.

Reason: The original clinical abstract identifies CRX as a photoreceptor homeodomain transcription factor, but full clinical Methods remain unavailable. Independent human regulatory-DNA and promoter assays establish the RNA polymerase II-specific child GO:0000981. Preserve the original NAS citation rather than claiming that its inaccessible full text directly supplied those later assays.

Proposed replacements: DNA-binding transcription factor activity, RNA polymerase II-specific

Summary: Retain the supported M1AP interaction as non-core.

Reason: PMID:16189514 has 1 positive literal interaction record(s) joining CRX to M1AP (Q8TC57); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported tax interaction as non-core.

Reason: PMID:22458338 has 3 positive literal interaction record(s) joining CRX to tax (P03410); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The HTLV-2 Tax association is retained as a viral interaction context; it does not establish infection of photoreceptors or a CRX antiviral function. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported PRKAB2 interaction as non-core.

Reason: PMID:24722188 has 1 positive literal interaction record(s) joining CRX to PRKAB2 (O43741); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. PRKAB2 is a noncatalytic AMPK scaffold subunit; binding it does not establish binding to the catalytic kinase subunit. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured ROR2 association by its supported partner class.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to ROR2 (A1L4F5); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The partner is ROR2, a receptor tyrosine kinase with experimentally reported activity and also low-activity assay caveats. This class refinement does not claim that the interaction activates ROR2 or identifies a kinase-domain contact. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: receptor tyrosine kinase binding

Summary: Retain the supported PRKAB2 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to PRKAB2 (O43741); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. PRKAB2 is a noncatalytic AMPK scaffold subunit; binding it does not establish binding to the catalytic kinase subunit. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured GCM2 association by its supported partner class.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to GCM2 (O75603); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured STK16 association by its supported partner class.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to STK16 (O75716); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. STK16 has experimentally supported protein serine/threonine kinase activity. Binding to that kinase class does not imply phosphorylation of CRX or kinase regulation. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: protein serine/threonine kinase binding

Summary: Retain the supported ATG12 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to ATG12 (O94817); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured CCNC association by its supported partner class.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to CCNC (P24863); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. CCNC is cyclin C, independently characterized as a CDK8/CDK19 regulator. The specific ligand class is cyclin binding, not a claim that CRX activates a kinase. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: cyclin binding

Summary: Retain the supported CA8 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to CA8 (P35219); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. CA8 is explicitly catalytically inactive as a carbonic-anhydrase-related protein; an enzyme-binding refinement would be misleading. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured SOX5 association by its supported partner class.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to SOX5 (P35711); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured PSMB10 association by its supported partner class.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to PSMB10 (P40306); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. PSMB10 is a catalytic proteasome beta subunit with threonine-endopeptidase annotation. Protease binding describes the partner class without assigning proteolysis to CRX. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: protease binding

Summary: Retain the supported EIF5A interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to EIF5A (P63241); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured TLE5 association by its supported partner class.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to TLE5 (Q08117); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The partner has independently supported transcriptional corepressor function. The screen establishes binding, not transcriptional repression by the CRX-partner pair. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: transcription corepressor binding

Summary: Retain the supported DELE1 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to DELE1 (Q14154); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. DELE1 activates a protein kinase, but is not itself that kinase; kinase binding is not inferred. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported UBXN2B interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to UBXN2B (Q14CS0); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured LONRF1 association by its supported partner class.

Reason: PMID:25416956 has 2 positive literal interaction record(s) joining CRX to LONRF1 (Q17RB8); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner record identifies a ubiquitin-protein ligase; LONRF1 class support is phylogenetic, while ARIH2 and LNX1 have their own ligase evidence. This refines partner class and does not claim CRX ubiquitination or ligase regulation. Literal construct features include sufficient binding region:358-773. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: ubiquitin protein ligase binding

Summary: Retain the supported QRICH1 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to QRICH1 (Q2TAL8); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. QRICH1 has transcriptional and protein-homeostasis functions, but its precise DNA-binding versus coregulatory mode is not resolved by this pairwise screen. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported SZT2 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to SZT2 (Q5T011-5); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Literal construct features include sufficient binding region:2797-3375. The exact Q5T011-5 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported KLHL32 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to KLHL32 (Q5THT1); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported MLLT6 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to MLLT6 (Q6P2C6); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported LARP4 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to LARP4 (Q71RC2-6); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Literal construct features include sufficient binding region:1-374. The exact Q71RC2-6 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported PID1 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to PID1 (Q7Z2X4); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported C9orf72 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to C9orf72 (Q96LT7); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported GUCD1 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to GUCD1 (Q96NT3); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported PPP1R16B interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to PPP1R16B (Q96T49); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. PPP1R16B regulates a phosphatase; it is not itself the catalytic phosphatase, so phosphatase-binding specificity is not inferred. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported AIRIM interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to AIRIM (Q9NX04); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported ABI2 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to ABI2 (Q9NYB9); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured OSGIN1 association by its supported partner class.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to OSGIN1 (Q9UJX0); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner function documents a catalytic enzyme. No more precise retrieved enzyme-binding child fits this enzyme class, and neither its catalytic activity nor substrate pathway is assigned to CRX. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: enzyme binding

Summary: Retain the supported NIP7 interaction as non-core.

Reason: PMID:25416956 has 3 positive literal interaction record(s) joining CRX to NIP7 (Q9Y221); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured GCM2 association by its supported partner class.

Reason: PMID:25910212 has 3 positive literal interaction record(s) joining CRX to GCM2 (O75603); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the supported CA8 interaction as non-core.

Reason: PMID:25910212 has 3 positive literal interaction record(s) joining CRX to CA8 (P35219); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. CA8 is explicitly catalytically inactive as a carbonic-anhydrase-related protein; an enzyme-binding refinement would be misleading. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured SMAD3 association by its supported partner class.

Reason: PMID:25910212 has 3 positive literal interaction record(s) joining CRX to SMAD3 (P84022); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. SMAD3 is an independently established receptor-regulated SMAD; the specific R-SMAD binding class describes the bound partner without asserting CRX participation in TGF-beta signaling. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: R-SMAD binding

Summary: Retain the supported BANP interaction as non-core.

Reason: PMID:26871637 has 3 positive literal interaction record(s) joining CRX to BANP (A0A0S2Z5G4); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. This is an unreviewed BANP product with its own exact sequence; no functional equivalence to a differently numbered BANP product is presumed. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported ZNF688 interaction as non-core.

Reason: PMID:26871637 has 3 positive literal interaction record(s) joining CRX to ZNF688 (A0A0S2Z6P0); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The exact short unreviewed ZNF688 product is preserved; a zinc-finger gene label is not sufficient to infer a transcription-factor binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported BANP interaction as non-core.

Reason: PMID:26871637 has 3 positive literal interaction record(s) joining CRX to BANP (B4DE54); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. This is an unreviewed BANP product with its own exact sequence; no functional equivalence to a differently numbered BANP product is presumed. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported ACBD4 interaction as non-core.

Reason: PMID:26871637 has 3 positive literal interaction record(s) joining CRX to ACBD4 (K7EM05); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported HGS interaction as non-core.

Reason: PMID:26871637 has 3 positive literal interaction record(s) joining CRX to HGS (O14964); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured SMUG1 association by its supported partner class.

Reason: PMID:26871637 has 3 positive literal interaction record(s) joining CRX to SMUG1 (Q53HV7); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner function documents a catalytic enzyme. No more precise retrieved enzyme-binding child fits this enzyme class, and neither its catalytic activity nor substrate pathway is assigned to CRX. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: enzyme binding

Summary: Retain the supported BANP interaction as non-core.

Reason: PMID:26871637 has 3 positive literal interaction record(s) joining CRX to BANP (Q8N9N5-2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The BANP product is retained exactly. The record combines DNA/RNA-binding and transcriptional functions; this review does not assume all tested splice products share an independently established transcription-factor mechanism. The exact Q8N9N5-2 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported BANP interaction as non-core.

Reason: PMID:26871637 has 3 positive literal interaction record(s) joining CRX to BANP (Q8N9N5-7); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The BANP product is retained exactly. The record combines DNA/RNA-binding and transcriptional functions; this review does not assume all tested splice products share an independently established transcription-factor mechanism. The exact Q8N9N5-7 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured GCM2 association by its supported partner class.

Reason: PMID:29892012 has 1 positive literal interaction record(s) joining CRX to GCM2 (O75603); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the supported ABI2 interaction as non-core.

Reason: PMID:29892012 has 2 positive literal interaction record(s) joining CRX to ABI2 (Q9NYB9); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported PRKAB2 interaction as non-core.

Reason: PMID:31515488 has 2 positive literal interaction record(s) joining CRX to PRKAB2 (O43741); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. PRKAB2 is a noncatalytic AMPK scaffold subunit; binding it does not establish binding to the catalytic kinase subunit. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured GCM2 association by its supported partner class.

Reason: PMID:31515488 has 1 positive literal interaction record(s) joining CRX to GCM2 (O75603); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured CCNC association by its supported partner class.

Reason: PMID:31515488 has 1 positive literal interaction record(s) joining CRX to CCNC (P24863); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. CCNC is cyclin C, independently characterized as a CDK8/CDK19 regulator. The specific ligand class is cyclin binding, not a claim that CRX activates a kinase. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: cyclin binding

Summary: Retain the supported CA8 interaction as non-core.

Reason: PMID:31515488 has 1 positive literal interaction record(s) joining CRX to CA8 (P35219); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. CA8 is explicitly catalytically inactive as a carbonic-anhydrase-related protein; an enzyme-binding refinement would be misleading. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured SOX5 association by its supported partner class.

Reason: PMID:31515488 has 1 positive literal interaction record(s) joining CRX to SOX5 (P35711); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured ROR2 association by its supported partner class.

Reason: PMID:31515488 has 1 positive literal interaction record(s) joining CRX to ROR2 (Q01974); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The partner is ROR2, a receptor tyrosine kinase with experimentally reported activity and also low-activity assay caveats. This class refinement does not claim that the interaction activates ROR2 or identifies a kinase-domain contact. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: receptor tyrosine kinase binding

Summary: Retain the supported PPP1R16B interaction as non-core.

Reason: PMID:31515488 has 1 positive literal interaction record(s) joining CRX to PPP1R16B (Q96T49); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. PPP1R16B regulates a phosphatase; it is not itself the catalytic phosphatase, so phosphatase-binding specificity is not inferred. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported VPS37C interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to VPS37C (A5D8V6); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported SDCBP interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SDCBP (O00560); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported HGS interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to HGS (O14964); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported CIMIP4 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to CIMIP4 (O43247-2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. The exact O43247-2 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured TLX3 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to TLX3 (O43711); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the supported PRKAB2 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to PRKAB2 (O43741); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. PRKAB2 is a noncatalytic AMPK scaffold subunit; binding it does not establish binding to the catalytic kinase subunit. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured FOXH1 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to FOXH1 (O75593); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured GCM2 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to GCM2 (O75603); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the supported UBXN7 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to UBXN7 (O94888); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: The positive CRX–OR6B1 screen interaction is retained as non-core protein binding.

Reason: PMID:32296183 has three positive literal records for CRX and OR6B1 (UniProtKB:O95007), with matching participant sequences and retained assay features. The olfactory-receptor class is authentic, and GO:0031849 itself does not require agonism. Nevertheless, this isolated screen observation does not establish olfactory-receptor engagement as an informative biological function of CRX. Retain the supported generic association as non-core under the project instruction. This is a judgment about functional informativeness, not a claim that the interaction is false, that compartments prohibit binding, or that every partner-class refinement requires transfer of the partner activity.

Summary: Refine the measured ARIH2 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to ARIH2 (O95376); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner record identifies a ubiquitin-protein ligase; LONRF1 class support is phylogenetic, while ARIH2 and LNX1 have their own ligase evidence. This refines partner class and does not claim CRX ubiquitination or ligase regulation. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: ubiquitin protein ligase binding

Summary: Refine the measured SOX14 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SOX14 (O95416); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured TBX6 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to TBX6 (O95947); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the supported PRR35 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to PRR35 (P0CG20); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported LIMS4 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to LIMS4 (P0CW20); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported PNMA6A interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to PNMA6A (P0CW24); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured GYS1 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to GYS1 (P13807); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner function documents a catalytic enzyme. No more precise retrieved enzyme-binding child fits this enzyme class, and neither its catalytic activity nor substrate pathway is assigned to CRX. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: enzyme binding

Summary: Retain the supported LGALS3 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to LGALS3 (P17931); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported PSMA1 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to PSMA1 (P25786); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. PSMA1 is a proteasome alpha subunit; binding this noncatalytic component does not establish protease binding. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported NTF4 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to NTF4 (P34130); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured HNF1B association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to HNF1B (P35680); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured SOX5 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SOX5 (P35711-4); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The exact P35711-4 product sequence is verified; its function is not generalized to every isoform. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured SOX3 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SOX3 (P41225); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the supported CDKN2C interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to CDKN2C (P42773); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured SUOX association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SUOX (P51687); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner function documents a catalytic enzyme. No more precise retrieved enzyme-binding child fits this enzyme class, and neither its catalytic activity nor substrate pathway is assigned to CRX. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: enzyme binding

Summary: Refine the measured ATXN1 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to ATXN1 (P54253); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The partner has independently supported transcriptional corepressor function. The screen establishes binding, not transcriptional repression by the CRX-partner pair. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: transcription corepressor binding

Summary: Refine the measured SOX10 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SOX10 (P56693); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured IRX6 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to IRX6 (P78412); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured ROR2 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to ROR2 (Q01974); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The partner is ROR2, a receptor tyrosine kinase with experimentally reported activity and also low-activity assay caveats. This class refinement does not claim that the interaction activates ROR2 or identifies a kinase-domain contact. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: receptor tyrosine kinase binding

Summary: Refine the measured TLE5 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to TLE5 (Q08117-2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The partner has independently supported transcriptional corepressor function. The screen establishes binding, not transcriptional repression by the CRX-partner pair. The exact Q08117-2 product sequence is verified; its function is not generalized to every isoform. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: transcription corepressor binding

Summary: Refine the measured NFYC association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to NFYC (Q13952-2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The exact Q13952-2 product sequence is verified; its function is not generalized to every isoform. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured ZIC1 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to ZIC1 (Q15915); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured LONRF1 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to LONRF1 (Q17RB8); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner record identifies a ubiquitin-protein ligase; LONRF1 class support is phylogenetic, while ARIH2 and LNX1 have their own ligase evidence. This refines partner class and does not claim CRX ubiquitination or ligase regulation. Literal construct features include gal4 dna binding domain:n-n|sufficient binding region:358-773; sufficient binding region:358-773. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: ubiquitin protein ligase binding

Summary: Retain the supported QRICH1 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to QRICH1 (Q2TAL8); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. QRICH1 has transcriptional and protein-homeostasis functions, but its precise DNA-binding versus coregulatory mode is not resolved by this pairwise screen. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured TNS2 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to TNS2 (Q63HR2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. TNS2 has experimentally supported protein tyrosine phosphatase activity. The tested fragment is retained in the provenance; the binding result does not show CRX dephosphorylation or define the contact domain. Literal construct features include gal4 dna binding domain:n-n|sufficient binding region:125-1409; sufficient binding region:125-1409. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: protein phosphatase binding

Summary: Retain the supported KANK2 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to KANK2 (Q63ZY3); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported FAAP20 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to FAAP20 (Q6NZ36-4); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. The exact Q6NZ36-4 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported ZNF483 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to ZNF483 (Q6P088); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured POGZ association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to POGZ (Q7Z3K3); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. POGZ carries a phylogenetically curated DNA-binding transcription-factor class. The broader DNA-binding transcription-factor binding term avoids inventing RNA polymerase II specificity from this screen alone. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: DNA-binding transcription factor binding

Summary: Retain the supported IGFN1 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to IGFN1 (Q86VF2-5); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Literal construct features include gal4 dna binding domain:n-n|sufficient binding region:2841-3708; sufficient binding region:2841-3708. The exact Q86VF2-5 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported SMAP1 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SMAP1 (Q8IYB5-2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. The exact Q8IYB5-2 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported CFAP206 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to CFAP206 (Q8IYR0); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported BOD1L2 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to BOD1L2 (Q8IYS8); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported ATP6V0D2 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to ATP6V0D2 (Q8N8Y2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported BANP interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to BANP (Q8N9N5-2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The BANP product is retained exactly. The record combines DNA/RNA-binding and transcriptional functions; this review does not assume all tested splice products share an independently established transcription-factor mechanism. The exact Q8N9N5-2 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured LNX1 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to LNX1 (Q8TBB1); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner record identifies a ubiquitin-protein ligase; LONRF1 class support is phylogenetic, while ARIH2 and LNX1 have their own ligase evidence. This refines partner class and does not claim CRX ubiquitination or ligase regulation. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: ubiquitin protein ligase binding

Summary: Retain the supported M1AP interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to M1AP (Q8TC57); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported SMAP2 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SMAP2 (Q8WU79); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported TFG interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to TFG (Q92734); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured NEIL2 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to NEIL2 (Q969S2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner function documents a catalytic enzyme. No more precise retrieved enzyme-binding child fits this enzyme class, and neither its catalytic activity nor substrate pathway is assigned to CRX. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: enzyme binding

Summary: Retain the supported MYO15B interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to MYO15B (Q96JP2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official MYO15B record has predicted motor features, but no motor-adaptor mechanism is established by this interaction. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported ZC3H10 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to ZC3H10 (Q96K80); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. ZC3H10 is characterized here as an RNA-binding regulator; zinc-finger content alone does not establish a DNA-binding transcription-factor class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured RHOXF2 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to RHOXF2 (Q9BQY4); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the supported MENT interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to MENT (Q9BUN1); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported C1orf50 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to C1orf50 (Q9BV19); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured GLIS2 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to GLIS2 (Q9BZE0); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Retain the supported BANF2 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to BANF2 (Q9H503-2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Literal construct features include gal4 dna binding domain:n-n|sufficient binding region:8-97; sufficient binding region:8-97. The exact Q9H503-2 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported MYOZ1 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to MYOZ1 (Q9NP98); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured TCF7L2 association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to TCF7L2 (Q9NQB0-10); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. Independent official partner annotation and function establish a sequence-specific RNA polymerase II transcription-factor class. The binding refinement does not assert that this particular screen pair regulates transcription together. The exact Q9NQB0-10 product sequence is verified; its function is not generalized to every isoform. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding

Summary: Refine the measured AASDHPPT association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to AASDHPPT (Q9NRN7); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The official partner function documents a catalytic enzyme. No more precise retrieved enzyme-binding child fits this enzyme class, and neither its catalytic activity nor substrate pathway is assigned to CRX. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: enzyme binding

Summary: Retain the supported SPG21 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SPG21 (Q9NZD8); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported SAE1 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SAE1 (Q9UBE0); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. SAE1 is part of a heterodimeric SUMO-activating enzyme; the screen does not establish binding to the intact active enzyme or its catalytic UBA2 subunit. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported SEC14L4 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SEC14L4 (Q9UDX3); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Literal construct features include gal4 dna binding domain:n-n|sufficient binding region:1-360; sufficient binding region:1-360; sufficient binding region:1-360|gal4 dna binding domain:n-n. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported C19orf25 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to C19orf25 (Q9UFG5); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Retain the supported CTNNA3 interaction as non-core.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to CTNNA3 (Q9UI47-2); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The positive association is retained, but the available partner and interaction evidence does not establish a more informative molecular mechanism or a sufficiently specific binding class. The exact Q9UI47-2 product sequence is verified; its function is not generalized to every isoform. Retention follows the project instruction for supported generic binding; it does not make this interaction a primary CRX function.

Summary: Refine the measured SUFU association by its supported partner class.

Reason: PMID:32296183 has 3 positive literal interaction record(s) joining CRX to SUFU (Q9UMX1); all 42 fields and explicit positive flags are retained. Product sequence checks agree with the recorded ROGIDs. The partner has independently supported transcriptional corepressor function. The screen establishes binding, not transcriptional repression by the CRX-partner pair. The assay is a heterologous interaction screen, not evidence for a native stable complex or transfer of the partner activity to CRX.

Proposed replacements: transcription corepressor binding

Summary: Nuclear localization is consistent with the inherited CRX activity.

Reason: The current exact CRX sequence descends from the literal PTN000677464 nuclear-location IBD without a mapped loss on its path. Human retinal organoid CRX chromatin occupancy and regulatory activity independently support the nuclear location. The extant donor list is preserved without treating its size as evidence quality.

Summary: The combined electronic nuclear localization is correct.

Reason: The source combines mouse Crx with the Otx homeobox record and UniProt location SL-0191. Nuclear transcriptional activity and chromatin occupancy in human retinal organoids support the assignment; the method identifiers are not mistaken for a separate localization experiment.

Summary: The mouse nuclear location transfers coherently to human CRX.

Reason: O54751 is the authenticated mouse Crx ortholog. Its current nucleus evidence and published retinal promoter-complex context agree with direct human CRX chromatin occupancy. Retain the original source identity and its species distinction.

Summary: Specify a RNA polymerase II transcription regulator complex.

Reason: The current mouse donor has experimentally curated transcription-factor-complex membership from PMID:15689355. Its Nr2e3-Crx interaction and promoter co-occupancy, together with bovine CRX-FIZ1 complexes, support the RNA polymerase II-specific child GO:0090575. This does not assert fixed stoichiometry or an obligatory invariant assembly.

Proposed replacements: RNA polymerase II transcription regulator complex

Summary: The broad electronic transcription-regulation assignment is sound.

Reason: The original combined source names mouse Crx and IPR017970. Both the conserved homeodomain context and direct human CRX reporter experiments support transcription regulation. The source is retained at its broad precision; the existing RNA polymerase II-specific assertions supply more detailed coverage.

Summary: Specify RNA polymerase II transcription regulation.

Reason: The mouse O54751 transfer includes retinal gene-regulatory evidence from PMID:16574740. Human CRX independently binds regulatory DNA and alters RNA polymerase II promoter reporters. GO:0006357 provides supported process specificity without changing the positive source interpretation.

Proposed replacements: regulation of transcription by RNA polymerase II

Summary: Inherited RNA polymerase II transcription regulation is supported.

Reason: The literal PTN000677464 GO:0006357 IBD is present; the exact CRX sequence is inside its current descendant clade with no path loss record. Human reporter and organoid studies establish gene regulation in the target. Legitimate target experimental evidence is not circular, and downstream target directions are context dependent.

Summary: Retain the established visual-system role at transcriptional-program scope.

Reason: The clinical abstract connects CRX variants to cone-rod dystrophy and photoreceptor maintenance. Together with direct transcriptional evidence, this supports a visual-system contribution rather than photon detection by CRX itself. Full original clinical Methods were not recovered, so no additional original assay is inferred.

Summary: CRX transcriptional activity supports eye photoreceptor cell development.

Reason: Refine broad animal organ morphogenesis to GO:0042462 eye photoreceptor cell development, a current descendant of both GO:0009887 and GO:0046530. The original PMID:9390563 full text remains unavailable; its clinical abstract alone does not establish the anatomical mechanism. Independent human PMID:41418782 supplies the decisive evidence: CRX occupies regulatory DNA in retinal organoids, activates the RP1L1 promoter and represses PCDH8 in separate HEK293T assays, and its knockout causes loss of photoreceptor maturation markers and ectopic PROX1 in photoreceptor cells. CRX therefore performs transcriptional work within cell specialization rather than merely being a required substrate. Occupancy and sorted-cell RNA differences do not validate every target, and complete morphological maturation or direct causality for every peak is not claimed. Current mouse Nrl, Otx2 and Nr2e3 developmental annotations support the same-role convention; their underlying papers are not substituted for human evidence. This holistic refinement preserves the original source assertion and its access limit; it is not a reconstruction of the 1997 experiment or an additional NEW annotation.

Proposed replacements: eye photoreceptor cell development

Summary: The transferred nuclear-receptor binding class is supported.

Reason: The exact mouse Crx donor has nuclear-receptor binding evidence associated with RORbeta in PMID:16574740. Its complete abstract supports functional Crx-RORbeta cooperation but not every physical-assay detail; independently, PMID:15689355 explicitly reports Nr2e3-Crx two-hybrid and co-immunoprecipitation. Retain the class with curator deference at the unrecovered original-detail level, without relabeling the RORbeta source as Nr2e3.

Summary: Mouse nuclear-receptor interactions support the human binding class.

Reason: The original O54751 source is retained separately from the automatic transfer. Current donor records and the complete Nr2e3-Crx interaction abstract support nuclear-receptor binding; the RORbeta paper supplies a distinct retinal co-regulatory context. Neither a universal receptor complex nor a direct human assay is claimed.

Summary: CRX binds the NRL leucine zipper.

Reason: The original full paper maps the interaction using human NRL bait and bovine CRX library and deletion constructs, with negative controls and reciprocal pull-down experiments. This supports domain-specific binding, not an endogenous all-human complex. The current bounded IntAct/MINT target query did not return this old pair, which does not erase the directly read original evidence.

Summary: Human CRX positively regulates RNA polymerase II promoter activity.

Reason: Human CRX expression increased normalized arrestin and IRBP promoter CAT output, and an OTX-containing heterologous reporter responded specifically. The original positive assay remains correct despite repression of other targets in a later human organoid study.

Summary: The ARBA positive-transcription mapping is supported.

Reason: Current ARBA00027996 branch 45 matches the official CRX FunFam 1.10.10.60:FF:000068. Direct human CRX reporter activation independently establishes positive transcription regulation. A context-dependent repressive role does not negate this positive source assertion.

Summary: Bovine CRX reporter activation supports the positive transfer.

Reason: The literal Q9XSK0 donor has experimentally curated positive transcription regulation from PMID:18854042. The original bovine CRX/FIZ1 co-transfection experiments augment opsin promoter activation; independent human CRX reporter assays support transfer. The partner-dependent direction is not generalized to all CRX targets.

Summary: Retain transcription-factor binding with explicit source and corroboration scopes.

Reason: The literal bovine Q9XSK0 donor points to FIZ1 in PMID:18854042. That study directly establishes CRX-FIZ1 binding and coactivation, but does not test isolated sequence-specific FIZ1 DNA binding. The current FIZ1 record carries unrefuted DNA-binding IBA class annotations, whose phylogeny was not independently re-audited here. Separately, original PMID:10887186 demonstrates bovine CRX binding to human NRL, a sequence-specific RNA polymerase II regulator. These distinct premises support retaining the positive binding class without silently substituting NRL into the donor source tuple or asserting the no-direct-DNA-binding premise of GO:0001221.

Summary: CRX participates in promoter-associated transcription regulator complexes.

Reason: The literal bovine donor is supported by native retinal CRX-FIZ1 association and promoter-element complex experiments in PMID:18854042. Mouse promoter occupancy in that study and the separate Nr2e3-Crx work are corroborating contexts. Retain RNA polymerase II regulator-complex membership without asserting an obligatory stoichiometric enhanceosome.

Summary: Sequence-specific double-stranded DNA binding is independently established.

Reason: The original high-throughput SELEX study and its general Methods are available, but the CRX-specific supplementary construct/model record was not authenticated in this assessment. Retain the experimentally curated positive assertion with independent human CRX competition EMSA support from PMID:10625658. No CRX methylation preference, tested construct length, or target-table read is inferred from the general screen.