GATA2

Summary: GATA2 can repress polymerase II transcription as well as activate it.

Reason: The genuine GO:0000122 IBD is at AN0/PTN001600628, with the exact GATA2 target descending through AN219 and no recorded loss on its path. GATA2 activity is partner- and cell-context-dependent; evidence for transcriptional activation does not contradict an inherited repressive capacity. The original donor list is preserved and is not judged by donor count.

Summary: Cis-regulatory sequence-specific DNA binding is inherited and directly grounded in GATA2.

Reason: The actual PTHR10071 tree places the exact 480-residue human target at AN219 below the GO:0000978 IBD at AN0/PTN001600628. The retained target path has no negative assertion. Direct human promoter-binding and endothelial ChIP evidence independently supports the function. Donor count and the presence of target-derived experimental evidence are not reasons to discount the IBA.

Summary: The mouse orthology transfer agrees with direct human cis-regulatory DNA binding.

Reason: The current O09100 donor trace includes experimental GO:0000978 records from PMID:17962413 and PMID:21245044. This is a GO_REF:0000107 orthology transfer, not a new human assay. Independent human GATA2 promoter-binding and endogenous HMOX1 ChIP support the same molecular claim, while the original donor and Ensembl identifier remain literal.

Summary: The PAINT transcription-factor assertion is supported by actual ancestry and human experiments.

Reason: The genuine GO:0000981 IBD is at AN0/PTN001600628 and the exact human GATA2 sequence descends through AN219 without a target-path loss assertion. This phylogenetic placement is consistent with direct human cis-regulatory DNA binding and transcriptional regulation. Preserve the incoming WITH/FROM objects, including any target contribution to the ancestral experimental grounding.

Summary: GATA2 is a DNA-binding polymerase II transcription factor in endothelial cells.

Reason: The authentic PMID:27780851 abstract supports GATA2-dependent miR-126 transcription and related endothelial regulation, but the complete original assays and precise construct are not accessible in the inspected packet. Independent human GATA2 endogenous ChIP and gain/loss experiments establish the molecular function. Preserve the original IDA and its exact two-atom context; independent evidence does not make the uninspected source details verified.

Summary: GATA-family domains support the experimentally established RNA polymerase II transcription-factor activity.

Reason: The original InterPro IPR016374 electronic assertion is consistent with the GATA zinc-finger transcription-factor architecture. Human GATA2 promoter binding, reporter activation, endogenous ChIP and target-expression perturbation provide independent evidence that the protein regulates polymerase II transcription. Domain membership alone is not used to infer a particular endothelial target or natural isoform.

Summary: FOG1 is an informative transcription-coregulator partner of GATA2.

Reason: PMID:12483298 explicitly reports human FOG1 interaction with GATA1 and GATA2, rather than merely sharing a transcription-related title. The annotation names the actual coregulator-binding function and preserves Q8IX07 as the partner. The selected abstract establishes the interaction claim but does not establish exact natural isoform boundaries or every zinc-finger interface.

Summary: GATA2 binds transcriptional coactivators, with direct human CCAR1 evidence.

Reason: The literal annotation is an O09100/Ensembl orthology transfer; its current donor chain includes PMID:11724781. Independently, selected original PMID:23887938 Results and Figure 5 show GATA2 association with CCAR1, direct in-vitro interaction and enhancement of GATA2-dependent androgen-receptor transcriptional complexes. This supports coactivator binding without pretending that the donor experiment was performed on human GATA2.

Summary: Transcriptional activation is a directly supported GATA2 activity.

Reason: The O09100 donor trace contains transcription-activator experiments from PMID:16254139, PMID:7720565 and PMID:9305891. Human GATA2 promoter reporters and endogenous target regulation independently support polymerase II activation. Retain the transferred context, and do not interpret the activator term as excluding repression when GATA2 recruits different partners.

Summary: The rat donor experiment supports a context-specific neuronal migration role.

Reason: The actual Q924Y4 donor chain leads to PMID:21430145. Selected original Methods/Results quantify E16-to-E21 dorsal-midbrain neuronal migration in the developing superior colliculus after two Gata2 shRNAs and rescue with human GATA2; altered cell death did not explain the migration defect. This is stronger than expression correlation, but it remains a rodent developmental assay and not direct evidence for a human motor-protein activity. Preserve the original orthology relationship.

Summary: The broad DNA-binding assertion can be specified as cis-regulatory sequence-specific binding.

Reason: The mouse orthology assertion is biologically sound, but direct human GATA2 promoter DNA binding and endothelial ChIP establish the more informative regulatory DNA-binding activity. The replacement describes binding to polymerase II cis-regulatory DNA rather than generic affinity for nucleic acid. The original mouse donor assertion remains unchanged in the machine context.

Proposed replacements: RNA polymerase II cis-regulatory region sequence-specific DNA binding

Summary: GATA2 associates with regulatory chromatin in endothelial transcriptional control.

Reason: PMID:19242469 places GATA2 within VEGFR2 regulatory chromatin biology, and independent endogenous HMOX1 ChIP supports chromatin association. Retain this binding-context claim without treating every chromatin contact as transcriptional activation or inventing a narrower ancestry relation.

Summary: Chromatin association is supported without conflating it with a particular DNA motif.

Reason: The current O09100 donor chain includes chromatin-binding IDA records from PMID:18184866 and PMID:18779319. Human GATA2 ChIP independently demonstrates occupancy at endogenous regulatory chromatin. Retain the broad chromatin-association claim, while the sequence-specific regulatory activity is represented separately; no unverified hierarchical relationship between chromatin binding and a particular DNA-binding descendant is asserted.

Summary: The transcription-factor activity is specifically directed at polymerase II genes.

Reason: Selected original PMID:15016828 Methods and Results establish human GATA2-dependent KDR promoter activation, GATA-motif controls and GATA2-antibody-sensitive DNA complexes. Human Hex plasmids in the reporter experiments are distinct from the rat Hex adenovirus used in a later HUVEC experiment. These data and independent endogenous human endothelial ChIP support the polymerase II-specific transcription-factor activity. The original IDA is preserved; the verified ontology relation is GO:0000981 is_a GO:0003700. No modern natural-product identity is assigned to the expression construct.

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

Summary: The transcription-factor activity is specifically directed at polymerase II genes.

Reason: The authentic CYP2C19 paper explicitly reports GATA2 reporter activation even though its title foregrounds GATA4; the selected abstract does not establish that its GATA4/6 ChIP experiments also tested GATA2. Independent human GATA2 promoter binding, transcriptional reporters and endogenous ChIP establish GO:0000981. Preserve the original source/evidence and qualify the independent support rather than inventing an assay for the original paper.

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

Summary: The transcription-factor activity is specifically directed at polymerase II genes.

Reason: The incoming assertion is ARBA00028295/InterPro IPR039355 inference. Independent human GATA2 promoter binding, transcriptional reporters and endogenous ChIP establish GO:0000981. Preserve the original source/evidence and qualify the independent support rather than inventing an assay for the original paper.

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

Summary: Refine the verified PML interaction to transcription coactivator binding in the tested human-protein reporter context.

Reason: The newly acquired original shows reciprocal coimmunoprecipitation of human GATA2 and human PML in COS cells and GST/cellular-extract interface mapping. Human PML potentiates GATA2-dependent reporters in 293T cells; GATA-site mutations abolish the effect, while GATA2 abundance and DNA-binding controls are unchanged. These positive interaction and functional data support transcription coactivator binding (GO:0001223) rather than bare protein binding. The literal P29590-4 supporting entity is preserved, but the inspected historical construct is not independently sequence-mapped to that modern isoform. GST bait with cellular extract is not a purified two-component affinity assay. Initial endogenous hematopoietic-cell assays were unsuccessful; engineered Ba/F3 results and positive endogenous NB4 leukemia association are distinct contexts, and PML-RARalpha findings are not generalized to ordinary wild-type physiology.

Proposed replacements: transcription coactivator binding

Summary: The GATA2–ADH1A protein-binding claim remains unverified.

Reason: P07327 is human ADH1A. The authentic PMID:16153155 abstract describes DNA EMSA/supershift and transcriptional regulation; the full text is unavailable through the inspected publisher, repository and author-page routes. It does not allow verification or rejection of an additional protein-interaction assay. Preserve the IPI and literal ADH1A partner without alleging wrong-protein attribution or removing an experimental annotation from abstract-only evidence.

Summary: The source-specific PU.1/SPI1/P17947 interaction needs the original assay.

Reason: PMID:18250304 studies GATA2 mutations in CML transformation. Its authentic abstract reports altered transactivation and PU.1 inhibition, but does not resolve this particular PU.1/SPI1/P17947 interaction. The mutation paper may contain the relevant wild-type and binding controls outside the abstract. Retain UNDECIDED rather than infer absence, wrong partner or a coactivator-specific mechanism from incomplete access.

Summary: The source-specific CREBBP/Q92793 interaction needs the original assay.

Reason: PMID:18250304 studies GATA2 mutations in CML transformation. Its authentic abstract reports altered transactivation and PU.1 inhibition, but does not resolve this particular CREBBP/Q92793 interaction. The mutation paper may contain the relevant wild-type and binding controls outside the abstract. Retain UNDECIDED rather than infer absence, wrong partner or a coactivator-specific mechanism from incomplete access.

Summary: The positive SMAD4 interaction is retained as evidence, but bare protein binding is uninformative.

Reason: The exact PMID:20211142 GATA2–Q13485 pair is present in the retained IntAct records with two-hybrid and pull-down evidence, negative=false. The original study is an atlas of TF interactions. Removing GO:0005515 here is the generic-binding curation policy, not a claim that the interaction is false. A partner-specific regulatory MF requires independent functional interpretation of the interaction; no such replacement is inferred merely from both proteins being transcription factors.

Summary: Human GATA2 engages FOG2 as a transcription coregulator.

Reason: The original Methods identify full-length human GATA2 and human FOG2 constructs in mouse 3T3-L1 cells. FOG2 GATA-contact mutants reduce repression despite comparable expression, while GATA2-V296M alters proliferation and differentiation without simply abolishing the adipogenesis block. Together with the retained curator IPI for Q8WW38, this functional interface evidence supports transcription coregulator binding, GO:0001221, already accepted for another GATA2 partner. The mutations draw on previously characterized interaction surfaces; this paper is not claimed to supply a new purified two-protein affinity measurement. Preserve the literal partner and evidence code, and do not transfer CTBP enzymatic or metabolic-sensor activity to GATA2.

Proposed replacements: transcription coregulator binding

Summary: The observed GATA2–SMAD4 association does not justify retaining bare protein binding.

Reason: The exact PMID:21988832 pair is present in retained IntAct anti-tag coimmunoprecipitation and two-hybrid records with negative=false. These positive records are preserved. GO:0005515 gives no informative molecular role, and the present selected reading does not establish a more specific function performed by GATA2 through this pair. Removal is of the uninformative annotation, not the interaction evidence.

Summary: The functional GATA2 interaction with androgen receptor can be described as transcription-factor binding.

Reason: Selected original PMID:23887938 Results and Figure 5 show GATA2–AR association and its enhancement by CCAR1, together with GATA-motif-dependent transcriptional synergy and regulatory DNA occupancy. P10275 is the AR partner named in the source. This supports the informative polymerase II-specific DNA-binding transcription-factor-binding term; it does not transfer AR ligand binding or CCAR1 adaptor function to GATA2.

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

Summary: The CCAR1 interaction supports transcription-coactivator binding.

Reason: Selected original PMID:23887938 Results and Figure 5 demonstrate GATA2 association with CCAR1, in-vitro binding to recombinant CCAR1 fragments, and CCAR1 enhancement of GATA2-dependent regulatory complexes. The informative role is coactivator binding rather than bare protein binding. The central CCAR1 interaction region is not a GATA2 residue or a natural-product identity claim.

Proposed replacements: transcription coactivator binding

Summary: The positive P25788 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive P36406 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive P60411 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive P86479 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved. Original S2G row 1883 names PRR20A/Entrez122183; current IntAct names P86479/PRR20C and explicitly retains Entrez122183 as an identity cross-reference. This establishes the retained gene-level correspondence, not independently verified clone-sequence equivalence.

Summary: The positive Q08379 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q13077 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q13643 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q6A162 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q6UY14-3 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q7Z3S9 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q99750 screen interaction is retained, but generic protein binding is removed.

Reason: The authentic original Table S2G and the exact-partner IntAct records support an HI-II-14 positive. The screen tested human ORFs as yeast fusion proteins, with individual quadruplicate retesting and identity checks; the table is not a native cellular-complex assay. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive P25788 screen interaction is retained, but generic protein binding is removed.

Reason: The exact-partner IntAct record documents a positive two-hybrid array interaction. This supports a tested physical association, while the presently inspected evidence does not establish a physiological molecular role for this pair. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive P36406 screen interaction is retained, but generic protein binding is removed.

Reason: The exact-partner IntAct record documents a positive two-hybrid array interaction. This supports a tested physical association, while the presently inspected evidence does not establish a physiological molecular role for this pair. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q08379 screen interaction is retained, but generic protein binding is removed.

Reason: The exact-partner IntAct record documents a positive two-hybrid array interaction. This supports a tested physical association, while the presently inspected evidence does not establish a physiological molecular role for this pair. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q13643 screen interaction is retained, but generic protein binding is removed.

Reason: The exact-partner IntAct record documents a positive two-hybrid array interaction. This supports a tested physical association, while the presently inspected evidence does not establish a physiological molecular role for this pair. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q7Z3S9 screen interaction is retained, but generic protein binding is removed.

Reason: The exact-partner IntAct record documents a positive two-hybrid array interaction. This supports a tested physical association, while the presently inspected evidence does not establish a physiological molecular role for this pair. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q99750 screen interaction is retained, but generic protein binding is removed.

Reason: The exact-partner IntAct record documents a positive two-hybrid array interaction. This supports a tested physical association, while the presently inspected evidence does not establish a physiological molecular role for this pair. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive A8MQ03 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved. Original HuRI names B8A4K4/ORF13662, whereas the current pair names A8MQ03; their retained identity fields share ENSG00000197191.4. This supports a source-specific gene-identity join while preserving the different accessions and leaving protein-sequence equivalence unproven.

Summary: The positive P35548 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q3LI59 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q3LI67 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q3SY46 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q8IUC1 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q8IUC2 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q8IUC3 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q93062-3 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive Q9BYR8 screen interaction is retained, but generic protein binding is removed.

Reason: The original retained HuRI MITAB and exact-partner IntAct entries preserve the positive human-ORF two-hybrid context. Original clone/isoform identifiers are retained; the assay host is yeast and is not evidence of an endogenous human complex. GO:0005515 is uninformative about the function of GATA2, so its removal follows the generic-binding policy without denying the measured interaction or inventing a more specific partner function. The literal partner suffix, when supplied, is preserved.

Summary: The positive partner evidence is preserved without retaining bare protein binding.

Reason: The exact PMID:35140242 / P08651 records were inspected and are not marked negative. The NFIC association includes an anti-tag coimmunoprecipitation record as well as proximity labeling. No demonstrated target-specific molecular role beyond the present interaction/proximity is assigned by this draft. Remove the uninformative GO:0005515 claim while retaining its source and partner context; this is not rejection of the experimental observation.

Summary: The positive partner evidence is preserved without retaining bare protein binding.

Reason: The exact PMID:35140242 / Q92793 records were inspected and are not marked negative. The retained CREBBP record is proximity-dependent biotin identification; proximity alone is not a purified direct-binding assay. No demonstrated target-specific molecular role beyond the present interaction/proximity is assigned by this draft. Remove the uninformative GO:0005515 claim while retaining its source and partner context; this is not rejection of the experimental observation.

Summary: The positive partner evidence is preserved without retaining bare protein binding.

Reason: The exact PMID:35512704 / Q13485 records were inspected and are not marked negative. The SMAD4 records include pull-down and BRET/proximity readouts, which are kept distinct. No demonstrated target-specific molecular role beyond the present interaction/proximity is assigned by this draft. Remove the uninformative GO:0005515 claim while retaining its source and partner context; this is not rejection of the experimental observation.

Summary: The positive partner evidence is preserved without retaining bare protein binding.

Reason: The exact PMID:38884001 / P08651 records were inspected and are not marked negative. The NFIC record is an anti-tag coimmunoprecipitation association. No demonstrated target-specific molecular role beyond the present interaction/proximity is assigned by this draft. Remove the uninformative GO:0005515 claim while retaining its source and partner context; this is not rejection of the experimental observation.

Summary: The positive partner evidence is preserved without retaining bare protein binding.

Reason: The exact PMID:38884001 / P25788 records were inspected and are not marked negative. The PSMA3 record is an anti-tag coimmunoprecipitation association. No demonstrated target-specific molecular role beyond the present interaction/proximity is assigned by this draft. Remove the uninformative GO:0005515 claim while retaining its source and partner context; this is not rejection of the experimental observation.

Summary: This specific GOLGA2 interaction is unresolved in the bounded source reading.

Reason: The current PMID:38884001 row specifies Q08379. The retained IntAct response contains 1000 records and is not a complete target inventory; it has no exact matching record in that bounded page. The original target-pair table has not yet been inspected. Do not interpret the missing bounded hit as absence or remove this experimental claim without adjudicating its positive evidence.

Summary: The positive partner evidence is preserved without retaining bare protein binding.

Reason: The exact PMID:38884001 / Q13643 records were inspected and are not marked negative. The FHL3 records are anti-tag coimmunoprecipitation associations. No demonstrated target-specific molecular role beyond the present interaction/proximity is assigned by this draft. Remove the uninformative GO:0005515 claim while retaining its source and partner context; this is not rejection of the experimental observation.

Summary: The positive partner evidence is preserved without retaining bare protein binding.

Reason: The exact PMID:7568177 / P25801 records were inspected and are not marked negative. The original partner P25801 is mouse Lmo2; mixed-species construct context is retained. Pull-down, coimmunoprecipitation and two-hybrid records support the interaction, without assigning every TAL1/E47/GATA1-complex activity to this GATA2 pair. No demonstrated target-specific molecular role beyond the present interaction/proximity is assigned by this draft. Remove the uninformative GO:0005515 claim while retaining its source and partner context; this is not rejection of the experimental observation.

Summary: Nuclear localization is inherited and directly corroborated for GATA2.

Reason: The actual nucleus IBD is AN0/PTN001600628 with the exact target at AN219 and no intervening negative assertion. Human endogenous ChIP and transcriptional DNA-binding evidence corroborate nuclear action. Preserve the literal is_active_in relation; do not automatically refine a root nuclear location to a subcompartment.

Summary: GATA2 nuclear localization is biologically well supported, with source access bounded.

Reason: The PMID:27780851 nuclear-localization panel itself is not accessible in the inspected abstract-only packet. Independent human GATA2 endogenous ChIP and transcriptional experiments support the location. Accept the true nuclear claim while preserving its endothelial-cell atom and explicitly not claiming that the original microscopy panel was inspected.

Summary: The curated electronic nuclear-location assertion agrees with direct GATA2 evidence.

Reason: The supplied combined orthology, InterPro and location-vocabulary sources are kept distinct in the original context. Human GATA2 chromatin occupancy and transcriptional activity independently support nuclear localization. Retain the root organelle claim under the organelle policy rather than replace it with nucleoplasm.

Summary: Nucleoplasmic GATA2 localization is consistent with its direct regulatory chromatin activity.

Reason: The original HPA-based IDA is retained as a localization assertion. The particular HPA image and antibody panel have not been independently inspected here, but human endogenous GATA2 ChIP and target-gene regulation provide independent support for nucleoplasmic action. Do not use that corroboration to certify the uninspected antibody assay.

Summary: The ARBA nucleoplasm inference agrees with human regulatory-chromatin evidence.

Reason: The supplied ARBA00026290 location inference is consistent with direct human endogenous GATA2 ChIP and polymerase II target regulation. This is a supported compartment claim without asserting membrane, luminal or organelle-specific transport activity.

Summary: The Reactome nucleoplasmic setting is biologically consistent with GATA2 transcriptional activity.

Reason: The official Reactome event R-HSA-8956568 takes the TAL1 core complex R-HSA-8956524 as an input; that complex contains the GATA1/GATA2/GATA3 set R-HSA-8956530, whose GATA2 member R-HSA-996735 maps explicitly to human UniProt P23769 residues 1–480. The event and target entity are in nucleoplasm. This is a verified target-component chain supporting the original TAS location, independently consistent with human GATA2 regulatory-chromatin experiments. The model uses alternative GATA members and does not establish that every cited experiment assayed every possible complex composition.

Summary: The Reactome nucleoplasmic setting is biologically consistent with GATA2 transcriptional activity.

Reason: The official Reactome binding event R-HSA-996755 has the GATA-protein set R-HSA-996770 as an input. Its explicit member R-HSA-996735 is human GATA2/P23769 residues 1–480 in nucleoplasm. This actual target chain supports the original TAS location and is independently consistent with endogenous human GATA2 chromatin experiments. The family-level FOG/GATA model is not treated as proof that every paralog pair or every individual source experiment has been tested.

Summary: GATA2 participates in transcription-regulatory complexes.

Reason: The mouse O09100 donor chain for GO:0005667 includes PMID:19323994, which describes the LMO4/SCL/GATA2/NLI transcriptional assembly. Independent human GATA2/AR/CCAR1 complex experiments support transcription-regulator-complex membership. Preserve the orthology provenance and do not claim that all partners or every assay use the same species, natural product or DNA target.

Summary: The source-specific endothelial cytoplasm localization remains unverified.

Reason: The complete PMID:27780851 localization experiment is inaccessible in the inspected packet. Nuclear activity does not exclude a cytoplasmic pool, but cannot substitute for evidence for that pool. Preserve the IDA and endothelial-cell atom without assuming a wrong location or using lack of a targeting signal as localization proof.

Summary: The established transcriptional regulation acts through polymerase II.

Reason: InterPro-based general transcriptional regulation is sound, but direct GATA2 promoter binding, reporter activation and endogenous target regulation support the more specific polymerase II process. Both activation and repression occur, so a single-direction replacement would lose genuine biology.

Proposed replacements: regulation of transcription by RNA polymerase II

Summary: Regulation of polymerase II transcription is the central GATA2 process.

Reason: The original ARBA assertion is consistent with direct GATA2 regulatory DNA binding and modulation of target transcription in human cells. Both transcriptional activation and context-dependent repression are retained. This is work performed by the gene product, rather than a process inferred solely from disease or knockout necessity.

Summary: GATA2 can promote stimulus-evoked calcium signaling through a mast-cell transcriptional program.

Reason: The Q924Y4 donor trace points to PMID:22390417, whose authentic abstract reports that GATA1/2 regulate RBL-2H3 degranulation, calcium responses and PLC-gamma1 transcription; mouse mast cells separately implicate GATA2. Retain the transferred regulatory outcome with its source limits. It does not establish GATA2 as a channel, calcium transporter or direct phospholipase.

Summary: Zinc coordination is intrinsic to the GATA DNA-binding domains.

Reason: The original InterPro IPR013088 inference is compatible with the two GATA zinc-finger regions in the verified sequence and with the established DNA-binding transcription-factor mechanism. Retain structural zinc binding; do not infer catalytic metal chemistry or a separate metal-homeostasis role.

Summary: GATA2-dependent developmental programs can influence tissue morphogenesis.

Reason: The broad electronic morphogenesis claim is consistent with distinct endothelial and neural developmental contexts, including human GATA2 rescue of rat dorsal-midbrain/superior-colliculus migration. Morphogenesis describes generation and organization of anatomical form; developmental involvement alone does not establish that another retained term is its ontology descendant. In particular, the inspected official is_a/part_of query gives no path from positive regulation of angiogenesis (GO:0045766) to GO:0009653. No supported strict descendant has been established for this broad assertion, so it remains non-core rather than being labeled TOO_GENERAL on biological similarity alone.

Summary: GATA2 positively regulates VEGFR2 expression in the specified endothelial context.

Reason: Selected original PMID:22499991 Results go beyond the abstract: GATA2-specific siRNA reduces VEGFR2, and GATA2/VEGFR2 gain-of-function rescue supports the regulatory chain. Preserve the two literal has_input/has_output P35968 atoms. This supports expression regulation by GATA2, but not an uninspected direct migration assay or all effects of miRNA-200b.

Summary: The four alternative target contexts cannot yet be independently adjudicated.

Reason: The authentic PMID:27780851 abstract establishes a GATA2–miRNA endothelial program, but it does not resolve all four target-specific gene-expression claims. These alternative target inputs differ from the independently accepted VEGFR2 context of PMID:22499991; acceptance of gene-expression regulation in general does not decide each target claim. Preserve the exact raw OR logic: four alternatives, each with a target input and endothelial-cell context. The flat extension schema cannot express these alternatives, so all eight atom occurrences remain in the logical source archive and this reason, without flattening or synthetic duplicate rows. This representation limit is separate from the unresolved experiments and is not a source defect. The unavailable full original, rather than an inferred negative result, limits adjudication.

Summary: The negative expression claim remains source-context-specific and unresolved.

Reason: PMID:27780851 is available only as an authentic abstract in the inspected source packet. Its discussion of the GATA2/miRNA program does not establish the precise negative-expression readout for the supplied miRNA/cell conjunction. Preserve the original two atoms and experimental claim without guessing the direction of the regulatory step from network membership.

Summary: Cell differentiation is true but subsumed by retained cell-fate and lineage claims.

Reason: The broad ARBA assertion is supported by lineage instruction and other differentiation experiments. The accepted GO:0045165 cell fate commitment is a verified direct part_of descendant of GO:0030154 cell differentiation; the retained eosinophil and adipocyte contexts supply additional lineage detail. The general term adds no distinct claim here. TOO_GENERAL records this entailment without declaring the electronic source false or selecting one lineage as an exhaustive replacement.

Summary: Gata2 expression responds to retinoid treatment in the rat donor context.

Reason: The Q924Y4 donor chain leads to PMID:11880336, whose authentic abstract reports retinoid agonist treatment lowering Gata2 mRNA in rat glomeruli. The current response-to-lipid definition includes a change in state or activity such as gene expression, so induction/repression is not categorically disallowed. Retain the limited response assertion without inferring lipid binding, direct sensing or a GATA2-specific perturbation assay.

Summary: GATA2 can instruct an eosinophil differentiation program in the tested progenitors.

Reason: The authentic PMID:12045236 abstract and F-read original describe GATA2-driven eosinophil colonies and IL-5 responsiveness in human cord-blood CD34 recipients, with separate mouse knockdown/rescue experiments. Recipient species does not prove the species or natural isoform of every expression construct. Retain a specific lineage-program role without treating all GATA2 functions as eosinophil-specific.

Summary: GATA2 supports mast-cell degranulation through regulatory gene expression.

Reason: The actual rat donor source PMID:22390417 reports GATA-dependent PLC-gamma1 expression, calcium responses and degranulation in RBL-2H3 cells, with a separate GATA2 role in mouse mast cells. The gene product participates through transcriptional regulation; it is not itself a granule fusion protein. The limited authentic abstract supports retention of this outcome without adding new machinery-level claims.

Summary: The source-specific endothelial migration readout remains unresolved.

Reason: The inspected original main Results establish GATA2/VEGFR2 expression and rescue in human dermal microvascular endothelial cells, with Matrigel vessel-formation readouts. They do not identify an independent GATA2-specific migration assay. The Discussion sentence about migration cites earlier papers 18 and 19, rather than reporting this source-specific IMP experiment. The relevant supplementary assay and exact migration readout were not recovered. Preserve the experimental assertion and its microvascular-cell/dermis/vascular-wound conjunction; this uncertainty concerns the narrower readout, not failure to inspect an image or a denial of endothelial function.

Summary: Sequence-specific DNA binding can be specified as binding polymerase II cis-regulatory DNA.

Reason: The combined rat orthology and InterPro inference is preserved as supplied. Independent human GATA2 promoter binding and endogenous ChIP identify the informative regulatory DNA context. The replacement does not assert that all DNA contacts have a transcriptional effect or assign an unverified natural isoform.

Proposed replacements: RNA polymerase II cis-regulatory region sequence-specific DNA binding

Summary: GATA2 inherits a cell-fate regulatory role supported by direct lineage evidence.

Reason: The genuine cell-fate IBD is at AN3/PTN000800998 rather than the family root; the exact target at AN219 is within that descendant clade without a path loss. Eosinophil lineage-instruction and neuronal differentiation evidence support a role in directing cell programs. Preserve the source-node placement and incoming donor set, rather than treating donor count as support strength.

Summary: GATA2 regulates adipocyte differentiation in a context-dependent direction.

Reason: The authentic PMID:20705609 abstract describes GATA2 interactions with FOG/CTBP-associated repression and inhibition of adipogenesis. The broad fat-cell-differentiation process is not synonymous with positive regulation of differentiation; a negative regulator can participate. Retain the measured program as non-core without inventing a specific interaction assay not read in the original.

Summary: The rat developmental experiments support positive neuronal differentiation.

Reason: The actual donor source PMID:21430145 includes reduced NeuN differentiation after Gata2 knockdown and rescue with human GATA2 in developing rat dorsal midbrain/superior colliculus. This supports the transferred positive differentiation claim. Its separate PC12 overexpression experiment inhibits NGF-induced neurites, so do not generalize one direction to all neuronal contexts or assign the phenotype to a current human natural isoform.

Summary: The neural Notch-inhibition claim needs its source-specific assay context.

Reason: The authentic PMID:16672344 abstract supports GATA2-dependent neural precursor cell-cycle and differentiation effects, but the selected evidence inspected so far does not establish the particular Notch-signaling readout. Retain the original IDA and acts_upstream_of_or_within relationship without equating the downstream phenotype with demonstrated regulation of Notch. The original full experimental context remains to be inspected; no wrong-gene inference is made.

Summary: The inherited proangiogenic role is consistent with direct endothelial GATA2 experiments.

Reason: GO:0045766 originates at AN209/PTN002560234 in the actual PAINT family, with AN219 human GATA2 inside the inheriting clade and no target-path negative assertion. Human endothelial knockdown/rescue and target regulation independently support angiogenic activity. Retain this context-dependent biological program without adding a separate proangiogenic ligand function.

Summary: Endothelial GATA2 supports a context-specific angiogenic program.

Reason: PMID:19242469 describes the balance between GATA2 and TFII-I at VEGFR2 regulation and angiogenic behavior. Independent human endothelial GATA2 gain/loss and rescue experiments in PMID:21788589 support a positive angiogenic role. This is an experimentally supported cellular program downstream of transcription-factor activity, not a separate receptor or angiogenic ligand activity. Preserve this source-specific IDA and the upstream relationship.

Summary: Human endothelial GATA2 supports angiogenic behavior.

Reason: Selected original PMID:21788589 Methods/Results show GATA2 loss impairing endothelial tube formation and a resistant GATA2 rescue of miRNA-24-mediated effects. The evidence is GATA2-specific, not solely a miRNA perturbation. Preserve the endothelial-cell extension and distinguish the PAK4/BAD branch from the GATA2/HMOX1 branch.

Summary: Positive transcriptional regulation can be specified to polymerase II.

Reason: The ARBA positive-transcription inference agrees with direct human GATA2 promoter reporters, endogenous ChIP and target-expression regulation. GO:0045944 expresses the supported polymerase II specificity. This does not erase the separately supported repressive capacity of GATA2 in other complexes.

Proposed replacements: positive regulation of transcription by RNA polymerase II

Summary: Positive polymerase II regulation is inherited and experimentally grounded.

Reason: The actual IBD is AN0/PTN001600628 and the verified target descends through AN219 without loss. The current global and retained-main donor set adds one ZFIN source absent from the incoming literal list; preserve both dated assertions rather than silently rewriting the original context. Independent human GATA2 transcription experiments support the function.

Summary: GATA2 positively regulates the endothelial VEGF-receptor transcriptional program.

Reason: Selected original PMID:15016828 shows human GATA2 activation of the KDR promoter, with GATA-site mutation controls, and inhibition of this program by Hex. The Fig. 3 human Hex plasmid experiments are distinct from Fig. 4 rat Hex adenovirus in HUVECs; endogenous HUVEC association and GATA2-antibody-sensitive DNA complexes provide additional regulatory context. These are positive transcriptional-function experiments, not a transfer of every Hex effect to GATA2. The original IDA and its source context remain unchanged.

Summary: GATA2 supports positive RNA polymerase II transcription in the ADH1A regulatory context.

Reason: The authentic PMID:16153155 abstract reports a positive ADH1A cis-element that increases reporter transcription and GATA2 EMSA/supershift binding within that element. Together with independently established GATA2 RNA polymerase II activation, this supports the biological claim and retains the original P07327 target context. The abstract alone does not verify a GATA2-specific perturbation or site-mutant experiment, and the full original remains unavailable. DNA-regulatory support does not establish the separate GATA2–ADH1A protein-interaction assertion, which remains unresolved.

Summary: GATA2 can activate CYP2C19 transcription in the reported reporter context.

Reason: The authentic PMID:20206639 abstract explicitly reports GATA2 activation of a CYP2C19 promoter reporter, despite foregrounding GATA4 in its title. Retain the transcriptional activation claim. The abstract assigns EMSA/ChIP findings to particular GATA factors, so it is not used to assert an unreported GATA2 ChIP or endogenous physiological control in every hepatic context.

Summary: GATA2 directly regulates an endothelial HMOX1 transcriptional target.

Reason: Selected original PMID:21788589 includes endogenous human GATA2 ChIP at HMOX1 regulatory DNA and GATA2 gain/loss effects on HMOX1 protein, alongside rescue experiments. Preserve both the HMOX1 input and endothelial-cell atoms. The endogenous ChIP evidence is distinct from ambiguous species wording for a separate GFP expression construct.

Summary: The transferred positive-transcription claim agrees with direct GATA2 regulatory activity.

Reason: The rat donor chain leads to PMID:11093771, whose authentic abstract describes promoter EMSA/decoy evidence involving GATA2, C/EBP and AP-1 at endothelin-B receptor regulation. The source emphasizes AP-1 and does not make every component equivalent. Independent human GATA2 reporter and ChIP evidence supports positive polymerase II regulation; retain the donor/source limits.

Summary: GATA2 participates in a transcriptional activator complex in neuronal lineage specification.

Reason: The authentic PMID:19323994 abstract describes LMO4/SCL/GATA2/NLI complex assembly controlling V2b-specific enhancers. This supports positive transcriptional regulation by the GATA2-containing complex. Preserve the original IGI partner P70662 and the supplied relationship; do not assign all complex activities to GATA2 or treat the neuronal context as a unique natural isoform.

Summary: GATA2 activates RNA polymerase II transcription in the endothelial VEGFR2 program.

Reason: The p190RhoGAP/GATA2/TFII-I study links GATA2 to VEGFR2 transcription, and independent GATA2-dependent promoter and expression experiments support transcriptional activation. The product performs the DNA-binding regulatory work, rather than merely being required for an endothelial phenotype. The original IMP and acts_upstream_of_or_within wording are retained.

Summary: System development is subsumed by the retained neuronal developmental claim.

Reason: GATA2-dependent neural and endothelial development supports the broad electronic assertion. The retained GO:0001764 neuron migration entails GO:0048731 through the verified path neuron migration part_of neuron differentiation, is_a neurogenesis, part_of nervous system development, is_a system development. The experimentally supported rat dorsal-midbrain phenotype with human GATA2 rescue therefore supplies a more informative asserted descendant. TOO_GENERAL does not reject the multi-system claim or infer participation from disease association alone.

Summary: The rat macrophage evidence supports positive regulation of phagocytosis.

Reason: The literal IEA transfer traces to rat Gata2/Q924Y4 and PMID:12933836. Its authentic abstract reports antisense reduction of uptake and increased uptake after Gata2 expression, providing perturbation evidence rather than expression correlation alone. Full original access is not yet recovered in the current reading packet. Retain the regulatory phenotype as non-core without making GATA2 a direct engulfment effector.

Summary: The rat macrophage evidence supports positive regulation of phagocytosis.

Reason: The literal ISS transfer traces to rat Gata2/Q924Y4 and PMID:12933836. Its authentic abstract reports antisense reduction of uptake and increased uptake after Gata2 expression, providing perturbation evidence rather than expression correlation alone. Full original access is not yet recovered in the current reading packet. Retain the regulatory phenotype as non-core without making GATA2 a direct engulfment effector.

Summary: Developmental regulation is subsumed by retained specific regulatory claims.

Reason: The broad ARBA assertion is true, but the retained GO:0045666 positive regulation of neuron differentiation is an official is_a descendant through regulation of neuron differentiation and regulation of cell differentiation to GO:0050793. The source-specific neuronal and endothelial regulatory judgments retain the biological detail. This is ontology subsumption of a true claim, not a negative judgment on electronic evidence.

Summary: GATA2 can promote the uptake component of phagocytosis in the rat donor assay.

Reason: The actual Q924Y4 donor source PMID:12933836 reports Gata2 loss/gain effects on macrophage uptake. This is consistent with positive regulation of engulfment, but the selected evidence remains abstract-level and does not identify the immediate target machinery. Preserve the transferred claim and distinguish regulatory participation from direct membrane-remodeling activity.

Summary: GATA2 contributes to vascular repair through endothelial transcriptional regulation.

Reason: Original PMID:22499991 human dermal microvascular endothelial experiments show GATA2 knockdown and resistant overexpression affecting VEGFR2 expression and vessel formation, with VEGFR2 rescue. The mouse dermal-wound experiments separately test the miR-200b/TNF axis and coordinated GATA2/VEGFR2 changes. Together with the source curator IMP, these findings support contextual contribution to new-vessel formation during vascular repair. Preserve the dermis extension; no GATA2-specific whole-wound closure rescue is claimed, and upstream miRNA effects are not all assigned to GATA2.

Summary: The HHEX partner supports an informative transcription-factor interaction.

Reason: Selected original PMID:15016828 independently tests human GATA2 after the initial GATA6-bait discovery: reciprocal tagged coimmunoprecipitation in COS7 cells and endogenous HUVEC nuclear coimmunoprecipitation support association with HHEX, while GATA-dependent reporter and DNA-binding assays establish the regulatory context. The informative molecular function is transcription-factor binding, with the original Q03014 partner retained. Human Hex plasmids and the separate rat Hex adenovirus experiment are distinguished; the nuclear-extract DNA assay is not a purified-protein affinity measurement.

Summary: The C2H2-domain specificity requires inspection beyond the FOG1 abstract.

Reason: The authentic PMID:12483298 abstract establishes FOG1–GATA2 interaction and describes a multi-zinc-finger FOG1 protein, but does not identify which FOG1 domain was tested as the binding surface. Do not infer C2H2-domain binding from partner architecture alone. Preserve the experimental row while the original domain-level experiment remains unverified.

Summary: The specific sprouting-migration readout cannot be resolved from the available abstract.

Reason: PMID:27780851 is authentic but full original assays remain inaccessible in the inspected packet. General endothelial or angiogenic effects do not verify this exact GATA2-specific sprouting-migration claim and its endothelial-cell extension. Retain uncertainty without rejecting the curator or inferring a wrong target.

Summary: Expression evidence alone does not settle the cochlear developmental role.

Reason: The rat Q924Y4 donor trace points to PMID:20006695, whose authentic abstract describes cochlear Gata2/Gata3/prestin expression changes across age, location and treatment. The selected evidence does not include a Gata2-specific developmental perturbation or demonstrate which cochlear developmental step it performs. Preserve the IEP-based source chain; do not call it a wrong-gene annotation or infer direct participation solely from expression.

Summary: Animal anatomical development is subsumed by retained neuronal development.

Reason: The true broad ARBA assertion is entailed by the retained GO:0001764 neuron migration through neuron differentiation and neurogenesis to nervous system development, which is_a GO:0160108 animal gross anatomical part developmental process. Each edge was checked in the official ontology. The more informative neuronal claim preserves its rat experimental and human-rescue scope; TOO_GENERAL adds no assertion that every organ or natural product was assayed.

Summary: Positive regulation of miRNA transcription is supported by ancestry and the endothelial source.

Reason: The actual IBD is AN209/PTN002560234 and the exact GATA2 target at AN219 descends without a path loss. The authentic PMID:27780851 abstract explicitly supports GATA2-dependent miR-126 transcription. Retain the incoming IBA context; unresolved details of the individual assays do not negate this independently described transcriptional role.

Summary: GATA2 can positively regulate miR-126 transcription in endothelial cells.

Reason: The authentic PMID:27780851 abstract explicitly describes this transcriptional regulation. Preserve the supplied miRNA and endothelial-cell conjunction and the source IDA. Full original methods and precise construct are not verified by the abstract, so no natural-product-specific or additional target claim is added.

Summary: GATA2 positively regulates miR-126 transcription in the retained endothelial context.

Reason: The authentic PMID:27780851 abstract reports GATA2-dependent miR-126 transcription in human umbilical vein endothelial cells. This row has the same miRNA-input/endothelial-cell conjunction as the accepted IDA context, so the biological claim is accepted consistently. The literal Q96SQ7 with-entity and IGI evidence remain unchanged. The detailed genetic-interaction experiment and constructs cannot be verified from the abstract because the full original was not recovered; this evidential limitation does not negate the independently supported claim or establish a natural-product-specific function.

Summary: The precise endothelial proliferation experiment remains inaccessible.

Reason: The PMID:27780851 abstract describes an angiogenic regulatory program, but does not allow verification of the exact GATA2-specific proliferation assay within sprouting angiogenesis. Preserve its endothelial-cell atom and experimental evidence. Broad angiogenesis support is not substituted for this narrower readout.

Summary: Sequence-specific DNA binding can be specified as binding polymerase II cis-regulatory DNA.

Reason: Original PMID:28473536 human-TF HT-SELEX and methyl-SELEX Methods use recombinant proteins and random DNA libraries. The recovered authentic workbook identifies the GATA2 eDBD construct in S1 row294 and positive target motifs in S2 rows8188 and8193. These support sequence-specific DNA binding, without a natural full-length isoform, GATA2 structure or endogenous localization claim. Preserve the original IDA. The cis-regulatory refinement is independently grounded in human GATA2 promoter, motif-control and endogenous ChIP experiments in PMID:15016828 and PMID:21788589; random-library selection alone does not establish that context. The official ontology contains an is_a path from GO:0000978 to GO:1990837.

Proposed replacements: RNA polymerase II cis-regulatory region sequence-specific DNA binding

Summary: Sequence-specific DNA binding can be specified as binding polymerase II cis-regulatory DNA.

Reason: The original source is ARBA00028376; it is not a direct assay. Independent human GATA2 promoter binding and endogenous ChIP identify the informative regulatory DNA context. The replacement does not assert that all DNA contacts have a transcriptional effect or assign an unverified natural isoform.

Proposed replacements: RNA polymerase II cis-regulatory region sequence-specific DNA binding

Summary: GATA2 can restrain neural precursor proliferation in the studied developmental context.

Reason: PMID:16672344 reports GATA2 gain/loss effects on neural precursor cell-cycle progression and differentiation, with Cyclin D1/p27 and Notch-associated changes. Retain the measured proliferation role as context-specific biology. This does not turn GATA2 into a cell-cycle enzyme, nor establish that every GATA2-expressing precursor responds in the same direction.

Summary: GATA2 supports endothelial survival in the studied miRNA-24/HMOX1 context.

Reason: Selected original PMID:21788589 Methods/Results show GATA2 knockdown increasing endothelial apoptosis and resistant-GATA2 rescue of the miRNA-24 phenotype. This supports the negative-apoptosis regulatory outcome with its endothelial-cell extension. Keep it as a cell-context consequence of GATA2 transcriptional activity, and distinguish the parallel PAK4/BAD pathway.