The androgen receptor (AR; NR3C4) is an intracellular steroid receptor with an N-terminal transcriptional activation domain containing a polymorphic polyglutamine tract, a zinc-finger DNA-binding domain and a C-terminal ligand-binding domain. Full-length AR recognizes androgens, moves between cytosolic and nuclear pools, binds regulatory DNA and recruits context-dependent coactivators or corepressors to control transcription. It supports male sexual differentiation, reproductive function and tissue-specific androgen responses. Alternative products, including AR-V7, can alter ligand dependence and transcriptional behavior. The disordered activation domain supports molecular condensation as one mode of receptor assembly. Loss-of-function variants cause androgen insensitivity, whereas expansion of the CAG-encoded polyglutamine tract causes spinal and bulbar muscular atrophy. Dysregulated AR signaling, including altered abundance, ligand responses and splice products, contributes to prostate cancer progression.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000122 negative regulation of transcription by RNA polymerase II | IMP PMID:12902338 Identification of glucocorticoid receptor domains involved i... | ACCEPT | Summary: negative regulation of transcription by RNA polymerase II β accept. Reason: The original IMP is retained as context-dependent negative transcriptional regulation by AR. The inspected source abstract names AR as well as glucocorticoid-receptor signaling; its title does not establish misattribution. Repression is compatible with the receptor transcription mechanism and distinct from its many activating contexts. Supporting Evidence: PMID:12902338 Liganded androgen receptor repressed TGF-beta transactivation |
| GO:0000785 chromatin | IBA GO_REF:0000033 | ACCEPT | Summary: chromatin β accept. Reason: Chromatin association is independently established in human AR studies, including ligand-dependent occupancy and coregulator recruitment. Retain the PAINT inference as a core location; target self-support is legitimate. The exact PTN002377694 tree/MSA placement has not been reconstructed, so this is not a claimed independent topology audit. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002377694 Β· PTN002377694 UNRESOLVED Original PAINT node retained; exact target-to-node topology/MSA not independently reconstructed. Target self-inclusion and donor count are not failure evidence; independent target biology is evaluated separately. |
| GO:0000785 chromatin | IDA PMID:17277772 Cooperative demethylation by JMJD2C and LSD1 promotes androg... | ACCEPT | Summary: chromatin β accept. Reason: PMID17277772 explicitly reports AR, JMJD2C and LSD1 assembly on chromatin at AR target genes. Retain receptor chromatin occupancy; the partner enzymes perform demethylation. Supporting Evidence: PMID:17277772 androgen receptor, JMJD2C and LSD1 assemble on chromatin |
| GO:0000785 chromatin | IDA PMID:17505061 Sirtuin 1 is required for antagonist-induced transcriptional... | ACCEPT | Summary: chromatin β accept. Reason: The original experimental chromatin annotation is coherent with the source-specific transcriptional coregulator work and independently demonstrated human AR chromatin occupancy. Retain without assigning a partner catalytic activity to AR. |
| GO:0000785 chromatin | ISA GO_REF:0000113 | ACCEPT | Summary: chromatin β accept. Reason: The TFClass ISA chromatin assignment fits the DNA-binding nuclear receptor and is independently supported by human target-gene occupancy studies. Retain the original TFClass provenance. |
| GO:0000976 transcription cis-regulatory region binding | IDA PMID:18487222 Prohibitin and the SWI/SNF ATPase subunit BRG1 are required ... | ACCEPT | Summary: transcription cis-regulatory region binding β accept. Reason: The inspected PMID18487222 promoter/ChIP experiments measure AR occupancy at PSA/KLK2 regulatory regions in prostate-cell systems. This supports cis-regulatory-region association; it is separate from the unresolved polymerase III assertion from that paper. |
| GO:0000976 transcription cis-regulatory region binding | IDA PMID:19886863 Androgen regulation of the prostatic tumour suppressor NKX3.... | ACCEPT | Summary: transcription cis-regulatory region binding β accept. Reason: The original PMID19886863 nuclear-receptor/DNA-regulatory experiments support AR action at transcriptional regulatory regions. This is a core receptor function; no cofactor catalytic activity is transferred. |
| GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding | IDA PMID:12799378 A direct beta-catenin-independent interaction between androg... | ACCEPT | Summary: RNA polymerase II transcription regulatory region sequence-specific DNA binding β accept. Reason: Retain the curated DNA-binding assertion because sequence-specific regulatory DNA recognition is an established human AR function. The PMID12799378 abstract specifically reports AR at a Tcf4-responsive c-myc element and direct ARβTcf4 interaction; ChIP alone does not resolve whether AR or Tcf4 makes each base contact there. Independent ARE-binding evidence is corroboration, not a claim that this ChIP proves an isolated interface. |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | IDA PMID:16728402 Glucocorticoid and androgen activation of monoamine oxidase ... | ACCEPT | Summary: RNA polymerase II cis-regulatory region sequence-specific DNA binding β accept. Reason: PMID16728402 supports sequence-specific AR action at a cis-regulatory target. Retain the experimental DNA-binding activity as central to receptor-mediated transcription. |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | IDA PMID:25802280 Loss of Androgen-Regulated MicroRNA 1 Activates SRC and Prom... | ACCEPT | Summary: RNA polymerase II cis-regulatory region sequence-specific DNA binding β accept. Reason: PMID25802280 links AR to target regulatory sequences in miRNA transcription. Retain the original cis-regulatory DNA-binding experiment as a manifestation of the core transcription factor activity. |
| GO:0000979 RNA polymerase II core promoter sequence-specific DNA binding | IEA GO_REF:0000107 | UNDECIDED | Summary: RNA polymerase II core promoter sequence-specific DNA binding β undecided. Reason: The exact mouse-derived core-promoter assertion and its donor experiment have not been inspected. Human AR binding to AREs/enhancers does not automatically establish this narrower core-promoter context. Preserve the IEA source and do not infer failure from species or donor count. |
| GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific | ISA GO_REF:0000113 | ACCEPT | Summary: DNA-binding transcription factor activity, RNA polymerase II-specific β accept. Reason: The TFClass assignment to a sequence-specific Pol II transcription factor is independently supported by human AR DNA-recognition and reporter/chromatin experiments. This is the central receptor activity. |
| GO:0001091 RNA polymerase II general transcription initiation factor binding | IPI PMID:20181722 TAF1 differentially enhances androgen receptor transcription... | ACCEPT | Summary: RNA polymerase II general transcription initiation factor binding β accept. Reason: PMID20181722 explicitly tests interaction of the AR N-terminal activation region with the general-transcription machinery component TAF1. Retain the specific binding term rather than infer TAF enzymatic activity. |
| GO:0001223 transcription coactivator binding | IDA PMID:10428808 Isolation and characterization of ARA160 as the first androg... | ACCEPT | Summary: transcription coactivator binding β accept. Reason: The actual PMID10428808 original binding and functional assays establish interaction of human AR with ARA160, a transcriptional coactivator. Preserve each distinct original assay row; AR binds the coactivator rather than becoming it. Supporting Evidence: PMID:10428808 The far-Western blotting and co-immunoprecipitation assays demonstrate that the AR can interact directly with ARA160/TMF. |
| GO:0001223 transcription coactivator binding | IPI PMID:10428808 Isolation and characterization of ARA160 as the first androg... | ACCEPT | Summary: transcription coactivator binding β accept. Reason: The actual PMID10428808 original binding and functional assays establish interaction of human AR with ARA160, a transcriptional coactivator. Preserve each distinct original assay row; AR binds the coactivator rather than becoming it. Supporting Evidence: PMID:10428808 The far-Western blotting and co-immunoprecipitation assays demonstrate that the AR can interact directly with ARA160/TMF. |
| GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific | IDA PMID:16728402 Glucocorticoid and androgen activation of monoamine oxidase ... | ACCEPT | Summary: DNA-binding transcription activator activity, RNA polymerase II-specific β accept. Reason: Retain the original PMID16728402 activator activity; the source-specific DNA-regulatory evidence supports AR performing transcriptional activation, not merely changing an indirect phenotype. |
| GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific | IDA PMID:25802280 Loss of Androgen-Regulated MicroRNA 1 Activates SRC and Prom... | ACCEPT | Summary: DNA-binding transcription activator activity, RNA polymerase II-specific β accept. Reason: Retain the original PMID25802280 activator activity in the miRNA regulatory context. The receptor supplies sequence-specific transcriptional regulation; no new process assertion is proposed. |
| GO:0003677 DNA binding | IEA GO_REF:0000002 | ACCEPT | Summary: DNA binding β accept. Reason: The InterPro DNA-binding assignment is an appropriate broad umbrella for the zinc-finger nuclear-receptor DNA-binding domain and independently established AR DNA recognition. Breadth alone is not evidence of a non-core or incorrect assertion. |
| GO:0003682 chromatin binding | IDA PMID:21730289 Regulation of androgen receptor-mediated transcription by RP... | ACCEPT | Summary: chromatin binding β accept. Reason: The original PMID21730289 chromatin-binding assertion agrees with receptor/coregulator occupancy at AR-regulated chromatin. Retain as a core binding context without converting partner recruitment into a catalytic activity of AR. |
| GO:0003700 DNA-binding transcription factor activity | IDA PMID:11477070 DJ-1 positively regulates the androgen receptor by impairing... | ACCEPT | Summary: DNA-binding transcription factor activity β accept. Reason: Retain the original experimental transcription-factor activity. Coregulator modulation in the cited study presupposes and experimentally measures AR-dependent transcription; the broad term remains a valid umbrella for the narrower Pol II-specific activity. |
| GO:0003700 DNA-binding transcription factor activity | IDA PMID:15572661 Negative modulation of androgen receptor transcriptional act... | ACCEPT | Summary: DNA-binding transcription factor activity β accept. Reason: Retain the original experimental transcription-factor activity. Coregulator modulation in the cited study presupposes and experimentally measures AR-dependent transcription; the broad term remains a valid umbrella for the narrower Pol II-specific activity. |
| GO:0003700 DNA-binding transcription factor activity | IEA GO_REF:0000120 | ACCEPT | Summary: DNA-binding transcription factor activity β accept. Reason: The combined electronic nuclear-receptor domain/ortholog assignment is independently corroborated by human AR DNA-binding and transcriptional experiments. No claim is made to have reconstructed the exact combined rule. |
| GO:0003707 nuclear steroid receptor activity | IDA PMID:12799378 A direct beta-catenin-independent interaction between androg... | ACCEPT | Summary: nuclear steroid receptor activity β accept. Reason: The cited source experimentally studies ligand-dependent AR transcription and receptor/coregulator interactions. Nuclear steroid receptor activity is the direct central function, distinct from secondary proliferation or tumor phenotypes. |
| GO:0003707 nuclear steroid receptor activity | IDA PMID:16120611 Modulation of androgen receptor transactivation by FoxH1. A ... | ACCEPT | Summary: nuclear steroid receptor activity β accept. Reason: The cited source experimentally studies ligand-dependent AR transcription and receptor/coregulator interactions. Nuclear steroid receptor activity is the direct central function, distinct from secondary proliferation or tumor phenotypes. |
| GO:0003707 nuclear steroid receptor activity | IEA GO_REF:0000117 | ACCEPT | Summary: nuclear steroid receptor activity β accept. Reason: The ARBA nuclear steroid receptor assertion is independently established by human androgen-binding and transcription studies. Retain the electronic source unchanged; this does not imply the exact rule derivation was audited. |
| GO:0004879 nuclear receptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: nuclear receptor activity β accept. Reason: PAINT nuclear receptor activity is strongly corroborated on human AR. A broad family node and target self-donor are not defects; retain the phylogenetic assertion while disclosing that full topology/MSA was not re-evaluated. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002377694 Β· PTN002377694 UNRESOLVED Original PAINT node retained; exact target-to-node topology/MSA not independently reconstructed. Target self-inclusion and donor count are not failure evidence; independent target biology is evaluated separately. |
| GO:0004879 nuclear receptor activity | IDA PMID:17277772 Cooperative demethylation by JMJD2C and LSD1 promotes androg... | ACCEPT | Summary: nuclear receptor activity β accept. Reason: The PMID17277772 experiments place ligand-bound AR on target genes with demethylase cofactors and measure receptor-dependent transcription. Retain nuclear receptor activity, without assigning demethylation to AR. |
| GO:0004879 nuclear receptor activity | IDA PMID:19244107 A novel androgen receptor splice variant is up-regulated dur... | ACCEPT | Summary: nuclear receptor activity β accept. Reason: PMID19244107 examines AR splice variants, including constitutive transcriptional activity of ligand-binding-domain-deficient products. Retain the receptor activity while distinguishing variant-specific hormone independence from full-length ligand regulation. |
| GO:0004879 nuclear receptor activity | IDA PMID:19886863 Androgen regulation of the prostatic tumour suppressor NKX3.... | ACCEPT | Summary: nuclear receptor activity β accept. Reason: Retain the original PMID19886863 receptor activity; its transcriptional mechanism agrees with the independently established human AR ligand/DNA-binding function. |
| GO:0004879 nuclear receptor activity | IDA PMID:20048160 Androgen receptor-dependent transactivation of growth arrest... | ACCEPT | Summary: nuclear receptor activity β accept. Reason: The original PMID20048160 functional receptor experiments support nuclear receptor activity. The regulatory cofactor or ligand context does not turn the annotation into a partner enzyme claim. |
| GO:0004879 nuclear receptor activity | IDA PMID:25091737 Identification of a new androgen receptor (AR) co-regulator ... | ACCEPT | Summary: nuclear receptor activity β accept. Reason: PMID25091737 reports AR ligand-binding-domain complexes, peptide modulation and receptor transcriptional readouts. Distinguish wild-type and antiandrogen-resistant variants; the shared nuclear receptor activity remains core. |
| GO:0004879 nuclear receptor activity | IEA GO_REF:0000120 | ACCEPT | Summary: nuclear receptor activity β accept. Reason: The electronic nuclear receptor assignment is independently supported by target-specific human binding/functional experiments. Preserve InterPro and ortholog evidence without claiming exact rule reconstruction. |
| GO:0004879 nuclear receptor activity | IMP PMID:19345326 Regulation of androgen receptor transcriptional activity and... | ACCEPT | Summary: nuclear receptor activity β accept. Reason: The actual PMID19345326 target-gene/reporters and RNF6 perturbations assay AR transcriptional receptor function. Ubiquitination regulates AR; AR is not the ubiquitin ligase. |
| GO:0004879 nuclear receptor activity | TAS PMID:15572661 Negative modulation of androgen receptor transcriptional act... | ACCEPT | Summary: nuclear receptor activity β accept. Reason: The PMID15572661 cited receptor/corepressor study is consistent with the established central nuclear receptor activity. Preserve its TAS evidence and do not relabel it as a newly performed direct assay. |
| GO:0005102 signaling receptor binding | IPI PMID:11875111 Inhibition of androgen receptor (AR) function by the reprodu... | MODIFY | Summary: signaling receptor binding β modify. Reason: The original PMID11875111 source reports direct ARβDAX-1 interactions and inhibition of AR activation/NβC interactions. DAX-1 is an atypical receptor acting as a non-DNA-binding repressive partner here; transcription corepressor binding describes the measured role more usefully than generic signaling receptor binding. No ligand activity is implied. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:11875111 We show that DAX-1 potently inhibits ligand-dependent transcriptional activation PMID:11875111 We provide evidence for direct interactions of the two receptors |
| GO:0005496 steroid binding | IEA GO_REF:0000002 | ACCEPT | Summary: steroid binding β accept. Reason: InterPro steroid binding is a valid broad umbrella for the ligand-binding domain. Direct androgen-binding experiments independently establish the target function; hormone-independent truncated isoforms do not invalidate the full-length activity. |
| GO:0005497 androgen binding | IDA PMID:12799378 A direct beta-catenin-independent interaction between androg... | ACCEPT | Summary: androgen binding β accept. Reason: Retain the original androgen-binding experiment. The PMID12799378 source distinguishes ligand conditions and beta-catenin recruitment, and androgen recognition is independently directly established for full-length human AR. |
| GO:0005497 androgen binding | IDA PMID:25091737 Identification of a new androgen receptor (AR) co-regulator ... | ACCEPT | Summary: androgen binding β accept. Reason: PMID25091737 explicitly studies DHT/wild-type receptor and antiandrogen/mutant ligand-binding-domain complexes. Retain androgen binding with those construct/ligand limits. |
| GO:0005497 androgen binding | IDA PMID:3353726 Molecular cloning of human and rat complementary DNA encodin... | ACCEPT | Summary: androgen binding β accept. Reason: The original PMID3353726 molecular characterization supports androgen receptor ligand binding. Retain the central activity, preserving original evidence and avoiding extension to ligand-binding-domain-deficient products. |
| GO:0005515 protein binding | IPI PMID:10075738 Cloning and characterization of androgen receptor coactivato... | MODIFY | Summary: protein binding β modify. Reason: The original PMID10075738 positive interaction and functional coactivation evidence identify ARA55 as an AR coactivator. Refine the binding term within the same source; AR is the receptor binding that cofactor. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:10075738 Yeast and mammalian two-hybrid systems and co-immunoprecipitation assays all prove ARA55 can bind to AR in a ligand-dependent manner. PMID:10075738 ARA55 can enhance AR transcriptional activity |
| GO:0005515 protein binding | IPI PMID:10930412 Androgen receptor interacts with a novel MYST protein, HBO1. | MODIFY | Summary: protein binding β modify. Reason: PMID10930412 identifies direct receptor association and transcriptional repression by HBO1/KAT7. Refine to corepressor binding in that tested context; do not infer acetyltransferase activity for AR or require every KAT7 context to be repressive. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:10930412 A ligand-enhanced interaction between AR and HBO1 was further confirmed in vivo and in vitro. PMID:10930412 HBO1 specifically repressed AR-mediated transcription |
| GO:0005515 protein binding | IPI PMID:10987273 Beta-catenin affects androgen receptor transcriptional activ... | MODIFY | Summary: protein binding β modify. Reason: PMID10987273 directly identifies beta-catenin in an AR-associated complex and its modulation of receptor activity. Beta-catenin binding is the source-specific partner term; no Wnt catalytic activity is assigned. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:10987273 Coimmunoprecipitation of beta-catenin with AR from LNCaP prostate cancer cells showed that the two molecules are present in the same complex. |
| GO:0005515 protein binding | IPI PMID:11477070 DJ-1 positively regulates the androgen receptor by impairing... | MODIFY | Summary: protein binding β modify. Reason: The original PMID11477070 PIASx/ARIP3 interaction and repressive functional context support corepressor binding. Preserve the measured partner and source rather than borrowing the mechanism from another screen. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:11477070 PIASx alpha inhibited the AR transcription activity in a dose-dependent manner PMID:11477070 restored AR transcription activity by absorbing PIASx alpha from the AR-PIASx alpha complex |
| GO:0005515 protein binding | IPI PMID:12864730 Isolation and identification of L-dopa decarboxylase as a pr... | MODIFY | Summary: protein binding β modify. Reason: The original PMID12864730 source identifies DDC binding to the AR N-terminal region and enhancement of AR activity. This supports coactivator binding in the stated context, not DDC catalytic activity for AR. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:12864730 DDC interacts with AR to enhance steroid receptor transactivation |
| GO:0005515 protein binding | IPI PMID:14645241 Interactions between activating signal cointegrator-2 and th... | KEEP AS NON CORE | Summary: protein binding β keep as non core. Reason: PMID14645241 describes ASC-2/NCOA6 association mediated by an Rb bridge. Retain the genuine regulatory-complex association as non-core; do not turn an explicitly indirect association into an isolated ARβNCOA6 interface or an AR adaptor mechanism. |
| GO:0005515 protein binding | IPI PMID:15563469 The molecular mechanisms of coactivator utilization in ligan... | MODIFY | Summary: protein binding β modify. Reason: PMID15563469 studies the receptor ligand-binding domain with coactivator motifs and functional modulation by NCOA2/TIF2. The source supports transcription coactivator binding, with motif/domain scope retained. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:15563469 the AR-LBD interacts with both FXXLF motifs and a subset of LXXLL motifs PMID:15563469 these LXXLL motifs are both necessary and sufficient for SRC-mediated AR regulation of transcription |
| GO:0005515 protein binding | IPI PMID:15572661 Negative modulation of androgen receptor transcriptional act... | MODIFY | Summary: protein binding β modify. Reason: The original PMID15572661 DAXX study reports direct AR association and transrepression. Corepressor binding is supported in that same source; it does not assign the partnerβs other activities to AR. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:15572661 Daxx functions as a negative AR coregulator through direct protein-protein interactions. |
| GO:0005515 protein binding | IPI PMID:16027218 Huntingtin interacting protein 1 modulates the transcription... | MODIFY | Summary: protein binding β modify. Reason: PMID16027218 describes HIP1 association with AR and positive receptor transcriptional function. Retain that source-local coactivator-binding interpretation rather than importing HIP1 endocytic activity into AR. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:16027218 HIP1 associates with the androgen receptor through a central coiled coil domain PMID:16027218 significantly repressing transcription when knocked down using a silencing RNA approach and activating transcription when overexpressed |
| GO:0005515 protein binding | IPI PMID:16051670 hZimp7, a novel PIAS-like protein, enhances androgen recepto... | MODIFY | Summary: protein binding β modify. Reason: The original PMID16051670 hZimp7/ZMIZ2 work identifies receptor association and coactivation. Refine to transcription coactivator binding, preserving the cellular/construct context. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:16051670 hZimp7 and the AR colocalize within the nucleus and form a protein complex at replication foci. PMID:16051670 hZimp7 augments the transcriptional activity of the AR |
| GO:0005515 protein binding | IPI PMID:16120611 Modulation of androgen receptor transactivation by FoxH1. A ... | MODIFY | Summary: protein binding β modify. Reason: The original PMID16120611 FOXH1 interaction is binding to a DNA-binding transcription factor. The specific Pol II DNA-binding transcription-factor binding term, already used for this same source elsewhere in the seed, is preferable to generic binding; co-repression does not make FOXH1 a non-DNA-binding corepressor. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:16120611 A protein-protein interaction was identified between the AR and FoxH1 independently of dihydrotestosterone. |
| GO:0005515 protein binding | IPI PMID:16461912 Cyclin D1b variant influences prostate cancer growth through... | KEEP AS NON CORE | Summary: protein binding β keep as non core. Reason: PMID16461912 explicitly distinguishes cyclin D1a from D1b: both associate with AR, but D1b has compromised repressive regulation. Retain the physical association without erasing isoform-dependent regulatory differences through an unconditional corepressor refinement. |
| GO:0005515 protein binding | IPI PMID:16494870 Androgen receptor auto-regulates its expression by a negativ... | KEEP AS NON CORE | Summary: protein binding β keep as non core. Reason: PMID16494870 directly reports IFI16 binding to the AR DNA-binding domain and effects on receptor expression. Retain the association as non-core; these data do not establish a new AR DNA-sensor or catalytic activity, and the exact repressive mechanism is not resolved by the abstract. |
| GO:0005515 protein binding | IPI PMID:16724108 Small carboxyl-terminal domain phosphatase 2 attenuates andr... | MODIFY | Summary: protein binding β modify. Reason: PMID16724108 identifies SCP2/CTDSP2 association and androgen-dependent recruitment, with perturbations showing repression of AR transcription. Corepressor binding is supported by that source. CTDSP2, not AR, supplies phosphatase activity. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:16724108 Small carboxyl-terminal domain (CTD) phosphatase 2 (SCP2) was identified and verified as a protein that interacts with the androgen receptor (AR). PMID:16724108 Silencing SCP2 and SCP1 by short hairpin RNAs increased androgen-dependent transcription of the PSA gene and augmented AR loading onto the PSA promoter and enhancer. |
| GO:0005515 protein binding | IPI PMID:16951154 Male germ cell-associated kinase, a male-specific kinase reg... | MODIFY | Summary: protein binding β modify. Reason: PMID16951154 combines ARβMAK coimmunoprecipitation with promoter recruitment, reporter enhancement and knockdown. Refine to coactivator binding in this nuclear regulatory context; MAK performs kinase chemistry. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:16951154 MAK physically associates with AR PMID:16951154 MAK is able to enhance AR transactivation potential |
| GO:0005515 protein binding | IPI PMID:17108144 Receptor for activated C kinase 1 (RACK1) and Src regulate t... | KEEP AS NON CORE | Summary: protein binding β keep as non core. Reason: The PMID17108144 abstract describes RACK1-mediated AR/Src signaling and a previously reported AR association. Retain the curated physical association as secondary regulatory context; RACK1 being a scaffold does not establish scaffold activity of AR. |
| GO:0005515 protein binding | IPI PMID:17170703 A novel function of caspase-8 in the regulation of androgen-... | MODIFY | Summary: protein binding β modify. Reason: PMID17170703 maps caspase-8/AR interaction motifs, shows loss of repression with binding-defective substitutions and separates the effect from caspase proteolysis. These source-local data support corepressor binding, not protease activity of AR. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:17170703 Substitutions of the amino-acid residues critical for AR-Casp8 interactions abolished the Casp8-mediated inhibition of AR transactivation. |
| GO:0005515 protein binding | IPI PMID:17183365 Control of prostate cell growth: BMP antagonizes androgen mi... | MODIFY | Summary: protein binding β modify. Reason: PMID17183365 reports physical Smad1βAR interaction and repression of receptor activity. Smad1 is a DNA-binding transcription factor; retain that partner class rather than transferring its BMP signaling role or calling AR a corepressor. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:17183365 Smad1 physically interacts with androgen-activated androgen receptor (AR) and suppresses its functions. |
| GO:0005515 protein binding | IPI PMID:17202144 Insulin-like growth factor 1/insulin signaling activates and... | MODIFY | Summary: protein binding β modify. Reason: PMID17202144 reports direct FOXO1βAR binding and promoter-associated antagonism. The seeded partner is the mouse Foxo1 accession, preserved as a heterologous partner; the receptor binds a DNA-binding transcription factor, with no human-partner or unique isoform claim. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:17202144 Foxo1 interacts directly with the C terminus of AR in a ligand-dependent manner |
| GO:0005515 protein binding | IPI PMID:17353003 A novel variant of the putative demethylase gene, s-JMJD1C, ... | MODIFY | Summary: protein binding β modify. Reason: PMID17353003 explicitly uses human AR bait and human s-JMJD1C, with GST and cellular interaction assays in its coactivator study. Refine to coactivator binding; the particular short JMJD1C variant remains part of the experiment scope, not an invented AR isoform. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:17353003 By using a fragment of the human AR (aa 325-919) as bait in a yeast two-hybrid screen, a region of the human JMJD1C gene was identified as interacting with AR. PMID:17353003 Here, we describe the discovery of a new AR coactivator which belongs to the JmjC containing enzyme family as a novel variant of JMJD1C |
| GO:0005515 protein binding | IPI PMID:17426252 Androgen-dependent gene expression of prostate-specific anti... | MODIFY | Summary: HIF1A association supports RNA polymerase II-specific DNA-binding transcription factor binding. Reason: Actual original publisher Results Cross Talk and Fig6A explicitly report reciprocal endogenous AR/HIF1alpha coimmunoprecipitation in LNCaP at 1% O2 plus DHT. This is physical association evidence separate from ChIP. Binding to a DNA-binding TF is the specific activity; purified binary contact and oxygen-sensing activity of AR are not asserted. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: file:human/AR/AR-notes.md The original Figure6A reciprocal immunoprecipitation identifies endogenous AR and HIF1alpha in the same complex in hypoxic, DHT-treated LNCaP cells; the promoter ChIP is a separate assay. |
| GO:0005515 protein binding | IPI PMID:17510388 DJ-1 binds androgen receptor directly and mediates its activ... | MODIFY | Summary: protein binding β modify. Reason: PMID17510388 explicitly reports direct DJ-1/PARK7 binding and modulation of AR transcription in hormone-treated prostate cells. Source-local coactivator binding captures the receptor role; partner localization changes do not establish all AR locations. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:17510388 This is the first evidence that DJ-1 directly interacts with AR. file:human/AR/AR-notes.md The independent prospective reviewer inspected the original PMID:17510388 Figure 4 caption and adjacent Results: DJ-1 overexpression increased AR reporter activity and knockdown decreased it without changing AR abundance. This supports a positive coregulatory interpretation beyond the direct-binding statement in the cached abstract. |
| GO:0005515 protein binding | IPI PMID:17909037 Peroxiredoxin 1 interacts with androgen receptor and enhance... | MODIFY | Summary: protein binding β modify. Reason: PMID17909037 combines reciprocal immunoprecipitation, ChIP and in-vitro pull-down with enhanced receptor transactivation, including antioxidant-deficient Prx1. Refine to coactivator binding without assigning peroxidase activity to AR. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:17909037 Reciprocal immunoprecipitation, chromatin immunoprecipitation, and in vitro pull-down assays corroborated that Prx1 interacts with AR and enhances its transactivation. |
| GO:0005515 protein binding | IPI PMID:18332867 Isosilybin B causes androgen receptor degradation in human p... | MODIFY | Summary: MDM2 association supports ubiquitin protein ligase binding. Reason: The complete original abstract explicitly reports antibody-pulled Akt/MDM2/AR complex under isosilybin B treatment in prostate cancer cells. Preserve treatment and substrate context. The target is binding an E3 partner, not enabling E3 chemistry. Full protocol uninspected. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: PMID:18332867 Antibody pull-down results also indicated that isosilybin B treatment enhances the formation of complex between Akt, Mdm2 and AR |
| GO:0005515 protein binding | IPI PMID:18451096 Leupaxin, a novel coactivator of the androgen receptor, is e... | MODIFY | Summary: protein binding β modify. Reason: PMID18451096 reports ligand-dependent leupaxinβAR association and AR coactivation. Refine the original interaction to coactivator binding; the paperβs separate adhesion/invasion effects do not make those AR molecular functions. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:18451096 leupaxin interacts with the androgen receptor in a ligand-dependent manner and serves as a transcriptional activator of this hormone receptor |
| GO:0005515 protein binding | IPI PMID:18451177 TRIM68 regulates ligand-dependent transcription of androgen ... | MODIFY | Summary: protein binding β modify. Reason: PMID18451177 reports TRIM68 interaction with AR and ligand-dependent receptor transactivation. Coactivator binding describes the tested regulatory role, without assigning TRIM68 ubiquitin-ligase chemistry to AR. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:18451177 interacts with AR and enhances transcriptional activity of the AR in the presence of dihydrotestosterone. |
| GO:0005515 protein binding | IPI PMID:18487222 Prohibitin and the SWI/SNF ATPase subunit BRG1 are required ... | MODIFY | Summary: BRG1/SMARCA4 association supports ATPase binding. Reason: The complete original abstract explicitly identifies BRG1 as the SWI/SNF ATPase and reports androgen-antagonist-induced physical AR/prohibitin/BRG1 association. Prior targeted original Methods/early Results corroborate this complex context. ATPase binding preserves the association without assigning remodeling catalysis to AR or requiring an isolated interface. Distinct p300 and PolIII claims remain unresolved. Proposed replacements: ATPase binding Supporting Evidence: PMID:18487222 Androgen antagonists induce recruitment of prohibitin and BRG1 to endogenous AR-responsive promoters and induce a physical association between AR and prohibitin and BRG1. |
| GO:0005515 protein binding | IPI PMID:18487222 Prohibitin and the SWI/SNF ATPase subunit BRG1 are required ... | UNDECIDED | Summary: protein binding β undecided. Reason: The inspected PMID18487222 passages expose p300 promoter occupancy, but the full pair-specific physical-interaction experiment has not been inspected. Preserve the IPI assertion as uncertain rather than promoting occupancy alone into a binding mechanism or borrowing another p300 paper. |
| GO:0005515 protein binding | IPI PMID:18640093 FOXP1 is an androgen-responsive transcription factor that ne... | MODIFY | Summary: protein binding β modify. Reason: PMID18640093 explicitly reports direct FOXP1βAR interaction and androgen-dependent repression, with a FOXP1 variant noted. Refine to DNA-binding transcription-factor binding; retain variant/context scope rather than recasting FOXP1 as a DNA-independent corepressor. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:18640093 FOXP1 directly interacts with AR and negatively regulates AR signaling ligand-dependently |
| GO:0005515 protein binding | IPI PMID:19345326 Regulation of androgen receptor transcriptional activity and... | UNDECIDED | Summary: protein binding β undecided. Reason: The PMID19345326 main text directly inspected here establishes RNF6 binding and ubiquitination; the specific RNF14/ARA54 recruitment experiment has not yet been located and read. Preserve this distinct partner assertion and uncertainty. The UniProt summary is corroboration, not a substitute for that experiment. |
| GO:0005515 protein binding | IPI PMID:19345326 Regulation of androgen receptor transcriptional activity and... | MODIFY | Summary: RNF6 association supports ubiquitin protein ligase binding. Reason: Actual cached GST-AR C-terminal capture, reciprocal tagged co-IP and endogenous CWR-R1/LNCaP Results were read. RNF6 is the E3 enzyme; AR is its bound regulated substrate. The separate RNF14 pair from this paper remains unresolved. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: PMID:19345326 We have identified a ubiquitin E3 ligase, RNF6, as an AR-associated protein in a proteomic screen. |
| GO:0005515 protein binding | IPI PMID:19481544 The histone methyltransferase, NSD2, enhances androgen recep... | MODIFY | Summary: protein binding β modify. Reason: The original PMID19481544 source identifies NSD2/WHSC1 as an AR-associated transcriptional coactivator. Refine to the binding role in that experiment, not histone methyltransferase activity for AR. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:19481544 NSD2 specifically interacts with the DNA-binding domain of androgen receptor (AR) via its HMG domain PMID:19481544 the over expression of NSD2, but not of NSD2 (DeltaSET) HMT-activity defective mutant, enhanced the mRNA level of PSA in a dose-dependent manner. |
| GO:0005515 protein binding | IPI PMID:19574450 Inhibition of prostate cancer cell growth by second-site and... | UNDECIDED | Summary: protein binding β undecided. Reason: The complete PMID19574450 abstract describes receptor antagonists and cofactor modulation but does not expose the gelsolin pair-specific experiment. The relevant assay/participant detail remains unread; neither absence from the abstract nor the drug-study title establishes a wrong interaction. |
| GO:0005515 protein binding | IPI PMID:19909775 TRIM24 mediates ligand-dependent activation of androgen rece... | MODIFY | Summary: protein binding β modify. Reason: PMID19909775 directly reports TRIM24 interaction with AR and enhanced androgen-dependent transcription. Refine to source-local coactivator binding; separate BRD7 repression does not reverse this partnerβs measured role. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:19909775 interacts with AR and enhances transcriptional activity of AR by dihydrotestosterone in prostate cancer cells. |
| GO:0005515 protein binding | IPI PMID:20478527 An integrated network of androgen receptor, polycomb, and TM... | MODIFY | Summary: protein binding β modify. Reason: PMID20478527 explicitly identifies ERG binding to and regulating AR in its prostate transcriptional network. ERG is a sequence-specific DNA-binding transcription factor; this refinement describes the original partner class without inventing an AR catalytic function. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:20478527 binding to and inhibiting AR activity at gene-specific loci |
| GO:0005515 protein binding | IPI PMID:20501646 The deubiquitinating enzyme USP26 is a regulator of androgen... | MODIFY | Summary: USP26 association supports enzyme binding. Reason: The complete original abstract explicitly reports USP26 binding through receptor-interaction motifs and counteraction of AR ubiquitination. Use enzyme binding for the partner class; AR is not a deubiquitinase. Full Methods were not independently inspected. Proposed replacements: enzyme binding Supporting Evidence: PMID:20501646 USP26 is a nuclear protein that binds to AR via three important nuclear receptor interaction motifs |
| GO:0005515 protein binding | IPI PMID:20541699 Regression of castrate-recurrent prostate cancer by a small-... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID20541699βs inspected abstract reports disruption of AR protein interactions by EPI-001 but does not identify the exact CREBBP assay. The original target-pair evidence remains uninspected, so an independent CBP coactivator literature cannot be silently substituted for it. |
| GO:0005515 protein binding | IPI PMID:20812024 FBI-1 functions as a novel AR co-repressor in prostate cance... | MODIFY | Summary: protein binding β modify. Reason: PMID20812024 identifies an AR/FBI-1/ZBTB7A interaction and a ternary repressive complex. ZBTB7A is a DNA-binding transcription factor, so use the corresponding partner-binding term rather than a non-DNA-binding corepressor category. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:20812024 A protein-protein interaction was identified between FBI-1 and AR in a ligand-dependent manner. |
| GO:0005515 protein binding | IPI PMID:21172304 BTG2 is an LXXLL-dependent co-repressor for androgen recepto... | MODIFY | Summary: protein binding β modify. Reason: PMID21172304 directly maps BTG2 LXXLL-dependent binding, binding-defective mutation and receptor repression. Refine to corepressor binding on those source-local results. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:21172304 BTG2 directly bound to the androgen receptor (AR) PMID:21172304 BTG2 bearing the mutant (92)LxxLL(96) motif failed to interact with AR. PMID:21172304 Androgen-induced promoter activation and expression of prostate-specific antigen (PSA) are significantly attenuated by BTG2. |
| GO:0005515 protein binding | IPI PMID:21242980 Inhibition of androgen receptor activity by histone deacetyl... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID21242980 Results show tagged and endogenous ARβHDAC4 coimmunoprecipitation plus in-vitro translated-protein capture and receptor repression. The functional effect is linked to SUMOylation rather than AR deacetylation; corepressor binding is supported without assigning either catalytic activity to AR. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:21242980 HDAC4 binds to and inhibits the activity of the AR. |
| GO:0005515 protein binding | IPI PMID:21242980 Inhibition of androgen receptor activity by histone deacetyl... | UNDECIDED | Summary: protein binding β undecided. Reason: The inspected PMID21242980 experiments demonstrate covalent AR SUMOylation, including denaturing capture and acceptor-site mutants. That does not by itself establish the noncovalent interaction meant by protein binding. The exact curated noncovalent-pair basis remains unresolved; preserve the source row without asserting every possible SUMO interaction is absent. |
| GO:0005515 protein binding | IPI PMID:21454491 Repression of androgen receptor activity by HEYL, a third me... | MODIFY | Summary: protein binding β modify. Reason: PMID21454491 reports HEYL interaction with the AR activation domain and transcriptional repression. HEYL is a DNA-binding transcription factor; the specific partner-class binding term is preferable to generic binding or a non-DNA-binding corepressor label. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:21454491 HEYL interacted with and repressed AR activation function-1 domain |
| GO:0005515 protein binding | IPI PMID:21512132 MST1 is a multifunctional caspase-independent inhibitor of a... | MODIFY | Summary: protein binding β modify. Reason: PMID21512132 combines ARβMST1/STK4 coimmunoprecipitation with transcriptional repression that is separable from kinase activity. Refine the binding to the demonstrated repressive coregulator context; no AR kinase activity is inferred. Proposed replacements: transcription corepressor binding Supporting Evidence: PMID:21512132 MST1 forms a protein complex with AR and antagonizes AR transcriptional activity |
| GO:0005515 protein binding | IPI PMID:21730179 Targeting the regulation of androgen receptor signaling by t... | MODIFY | Summary: FKBP4/FKBP52 association supports enzyme binding. Reason: The complete abstract and independently read original Results/Fig3 and main Methods establish FKBP52/AR/Hsp90 coassociation in LNCaP, LAPC4 and 22Rv1 cells. FKBP52 is a peptidyl-prolyl isomerase; enzyme binding captures the partner class while retaining complex-mediated scope. A direct AR BF3 contact was proposed but not demonstrated. Do not infer protein-folding chaperone binding from HSP90 membership, an AR isomerase activity, or a requirement for FKBP52 catalysis. Proposed replacements: enzyme binding Supporting Evidence: PMID:21730179 MJC13, inhibits AR function by preventing hormone-dependent dissociation of the Hsp90-FKBP52-AR complex |
| GO:0005515 protein binding | IPI PMID:21741601 Targeting androgen receptor in estrogen receptor-negative br... | MODIFY | Summary: protein binding β modify. Reason: The original PMID21741601 AR/beta-catenin study provides the specific partner relationship in its human breast-cell context. Refine generic binding to beta-catenin binding while retaining tissue and regulatory context. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:21741601 We detected the physical interaction between AR and Ξ²-catenin in the nuclear extracts of MDA-MB-453 breast cancer cells by co-immunoprecipitation |
| GO:0005515 protein binding | IPI PMID:21885566 The beta-catenin binding protein ICAT modulates androgen rec... | MODIFY | Summary: protein binding β modify. Reason: PMID21885566 examines beta-catenin-containing AR/ICAT assemblies and reports ARβbeta-catenin association. Refine to the actual partner class; complex cooperation is not a separate AR enzymatic activity. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:21885566 we detected the endogenous protein complex containing ICAT, AR, and Ξ²-catenin in prostate cancer cells using immunoprecipitation assays. PMID:21885566 ICAT enhances expression of endogenous PSA and KLK2, two androgen response genes |
| GO:0005515 protein binding | IPI PMID:22170608 Cryptochromes mediate rhythmic repression of the glucocortic... | UNDECIDED | Summary: protein binding β undecided. Reason: The inspected PMID22170608 abstract foregrounds mouse glucocorticoid receptor/cryptochrome biology. The specific ARβmouse Cry1 experiment has not been read. This is an access/scope gap, not evidence of paralog misattribution or grounds for experimental removal. |
| GO:0005515 protein binding | IPI PMID:22187462 Structural basis of coactivation of liver receptor homolog-1... | MODIFY | Summary: protein binding β modify. Reason: The PMID22187462 abstract explicitly reports AR binding tests involving beta-catenin mutants despite the title emphasizing LRH-1. Refine to beta-catenin binding on that own-source AR result; do not reject an experiment because another receptor dominates the title. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:22187462 The LRH-1 binding site in Ξ²-catenin is also required for association with androgen receptor |
| GO:0005515 protein binding | IPI PMID:22531786 A transcriptional repressor co-regulatory network governing ... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID22531786βs inspected summary establishes ERG/AR regulatory context but the distinct pair-specific physical assay has not yet been inspected. Keep this source row uncertain rather than borrow the experiment from PMID20478527. |
| GO:0005515 protein binding | IPI PMID:22722839 The mutational landscape of lethal castration-resistant pros... | MODIFY | Summary: KMT2D/MLL2 association supports histone methyltransferase binding. Reason: Actual own-paper Results and independently read official supplement Methods/S16 establish endogenous human VCaP association/reverse IP of AR with the methyltransferase KMT2D. Preserve complex-level assay scope, not purified binary contact or AR methyltransferase chemistry. Same-paper ERG evidence remains unresolved. Proposed replacements: histone methyltransferase binding Supporting Evidence: PMID:22722839 Reverse immunoprecipitation confirmed interactions between AR and MLL, MLL2, ASH2L and FOXA1 |
| GO:0005515 protein binding | IPI PMID:22722839 The mutational landscape of lethal castration-resistant pros... | UNDECIDED | Summary: protein binding β undecided. Reason: The PMID22722839 abstract reports AR association with an MLL regulatory complex. The exact ERG participant-specific assay is being checked in the actual full text; until that read resolves it, preserve this distinct original row as uncertain rather than infer a binary coregulator interface from a general complex description. |
| GO:0005515 protein binding | IPI PMID:22722839 The mutational landscape of lethal castration-resistant pros... | MODIFY | Summary: FOXA1 association supports RNA polymerase II-specific DNA-binding transcription factor binding. Reason: Actual own-paper Results and independently read official supplement Methods/S16 establish endogenous human VCaP association/reverse IP of AR with FOXA1. FOXA1 is a sequence-specific DNA-binding TF, so use TF binding rather than generic binding or coregulator binding. No purified interface claim. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:22722839 Reverse immunoprecipitation confirmed interactions between AR and MLL, MLL2, ASH2L and FOXA1 |
| GO:0005515 protein binding | IPI PMID:22722839 The mutational landscape of lethal castration-resistant pros... | MODIFY | Summary: KMT2A/MLL association supports histone methyltransferase binding. Reason: Actual own-paper Results and independently read official supplement Methods/S16 establish endogenous human VCaP association/reverse IP of AR with methyltransferase KMT2A. Preserve complex-level association and distinguish AR from the catalytic partner; do not borrow the unresolved ERG panel. Proposed replacements: histone methyltransferase binding Supporting Evidence: PMID:22722839 Reverse immunoprecipitation confirmed interactions between AR and MLL, MLL2, ASH2L and FOXA1 |
| GO:0005515 protein binding | IPI PMID:22722839 The mutational landscape of lethal castration-resistant pros... | KEEP AS NON CORE | Summary: protein binding β keep as non core. Reason: An independent targeted read of actual PMID22722839 Results and official supplement Methods/S16 verifies ASH2L in endogenous human VCaP AR coassociation/reverse immunoprecipitation. Retain this genuine complex association as non-core; detergent-lysate capture does not establish a purified binary interface or a new AR catalytic activity. The source-specific positive result is distinct from the still unresolved ERG panel. Supporting Evidence: file:human/AR/AR-notes.md It verified endogenous human VCaP AR coassociation/reverse immunoprecipitation for KMT2D, FOXA1, KMT2A and ASH2L. |
| GO:0005515 protein binding | IPI PMID:23260764 The androgen receptor induces a distinct transcriptional pro... | UNDECIDED | Summary: protein binding β undecided. Reason: The PMID23260764 abstract establishes FOXA1-dependent AR cistrome changes but the source-specific pair-binding assay is not exposed in the inspected text. Keep the curated interaction uncertain; pioneering activity and co-occupancy alone do not resolve a binary interface. |
| GO:0005515 protein binding | IPI PMID:23518348 The E3 ubiquitin ligase Siah2 contributes to castration-resi... | MODIFY | Summary: Siah2, original mouse accession Q06986 association supports ubiquitin protein ligase binding. Reason: Actual cached Results Siah2 Functions as an E3 Ubiquitin Ligase for AR and AR Contains Two Major Siah2-Binding Sites were read: tagged co-IP, AF2 pull-down and domain/mutant mapping. Preserve the original mouse Siah2 supporting entity; no donor-species replacement or AR E3 activity claim. Main Methods were read for cell models; full supplementary reagent provenance was not reconstructed. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: PMID:23518348 Analysis of AR immunoprecipitates showed that Siah2RM or Siah2WT bound to AR protein |
| GO:0005515 protein binding | IPI PMID:23566155 Ski-interacting protein (SKIP) interacts with androgen recep... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID23566155 reporter, coimmunoprecipitation and FRET Results support AR binding to SKIP/SNW1 in a coactivating context. Refine to coactivator binding while distinguishing tagged overexpression, prostate reporter cells and BHK imaging. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:23566155 SKIP is in a complex with the AR. PMID:23566155 SKIP augmented ligand- and AR-dependent transactivation in PC3 prostate cancer cells. |
| GO:0005515 protein binding | IPI PMID:23887938 CCAR1 promotes chromatin loading of androgen receptor (AR) t... | KEEP AS NON CORE | Summary: protein binding β keep as non core. Reason: PMID23887938 explicitly identifies CCAR1 as the protein directly contacting both AR and GATA2 and stabilizing their association. Retain the AR/GATA2 complex relationship without turning that bridge into a proven isolated ARβGATA2 interface or AR adaptor activity. |
| GO:0005515 protein binding | IPI PMID:23887938 CCAR1 promotes chromatin loading of androgen receptor (AR) t... | MODIFY | Summary: protein binding β modify. Reason: PMID23887938 directly identifies CCAR1 binding to AR and coactivation with recruitment of transcriptional machinery. Refine to source-specific coactivator binding; CCAR1-mediated bridging is not attributed to AR. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:23887938 CCAR1 interacted with and enhanced the transcriptional activity of AR. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID24728074 AR-specific Results explicitly identify LCK SH2-domain binding to synthetic phosphorylated AR peptides. Refine to SH2 domain binding, retaining the purified domain/phosphopeptide and affinity limits. This is not proof of endogenous full-length recruitment or the catalytic activity of the partner. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:24728074 Our assay detected multiple interactions with the peptide derived from Tyr(P)-267, including a relatively high affinity interaction with the SRC SH2 domain (KD = 1.85 ΞΌm) and weaker interactions with SH2 domains from other c-Src family kinase members, including YES1 and LCK. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID24728074 AR-specific Results explicitly identify YES1 SH2-domain binding to synthetic phosphorylated AR peptides. Refine to SH2 domain binding, retaining the purified domain/phosphopeptide and affinity limits. This is not proof of endogenous full-length recruitment or the catalytic activity of the partner. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:24728074 Our assay detected multiple interactions with the peptide derived from Tyr(P)-267, including a relatively high affinity interaction with the SRC SH2 domain (KD = 1.85 ΞΌm) and weaker interactions with SH2 domains from other c-Src family kinase members, including YES1 and LCK. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID24728074 AR-specific Results explicitly identify SRC SH2-domain binding to synthetic phosphorylated AR peptides. Refine to SH2 domain binding, retaining the purified domain/phosphopeptide and affinity limits. This is not proof of endogenous full-length recruitment or the catalytic activity of the partner. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:24728074 The peptide derived from Tyr(P)-362 interacted with SH2 domains from SRC, RASA1, PLCG1, and the PI3KR phosphatidylinositol kinase regulatory subunits. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID24728074 AR-specific Results explicitly identify PLCG2 SH2-domain binding to synthetic phosphorylated AR peptides. Refine to SH2 domain binding, retaining the purified domain/phosphopeptide and affinity limits. This is not proof of endogenous full-length recruitment or the catalytic activity of the partner. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:24728074 recruitment sites for domains from the phospholipases PLCG1 and PLCG2 were distributed throughout the length of the protein |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID24728074 AR-specific Results explicitly identify PLCG1 SH2-domain binding to synthetic phosphorylated AR peptides. Refine to SH2 domain binding, retaining the purified domain/phosphopeptide and affinity limits. This is not proof of endogenous full-length recruitment or the catalytic activity of the partner. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:24728074 recruitment sites for domains from the phospholipases PLCG1 and PLCG2 were distributed throughout the length of the protein |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID24728074 AR-specific Results explicitly identify RASA1 SH2-domain binding to synthetic phosphorylated AR peptides. Refine to SH2 domain binding, retaining the purified domain/phosphopeptide and affinity limits. This is not proof of endogenous full-length recruitment or the catalytic activity of the partner. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:24728074 The peptide derived from Tyr(P)-362 interacted with SH2 domains from SRC, RASA1, PLCG1, and the PI3KR phosphatidylinositol kinase regulatory subunits. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID24728074 AR-specific Results explicitly identify PTPN11 SH2-domain binding to synthetic phosphorylated AR peptides. Refine to SH2 domain binding, retaining the purified domain/phosphopeptide and affinity limits. This is not proof of endogenous full-length recruitment or the catalytic activity of the partner. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:24728074 Peptides derived from Tyr(P)-307, Tyr(P)-531, Tyr(P)-740, and Tyr(P)-774 recruited the PTPN11 protein-tyrosine phosphatase SH2 domain |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | MODIFY | Summary: protein binding β modify. Reason: Actual PMID24728074 AR-specific Results explicitly identify PIK3R3 SH2-domain binding to synthetic phosphorylated AR peptides. Refine to SH2 domain binding, retaining the purified domain/phosphopeptide and affinity limits. This is not proof of endogenous full-length recruitment or the catalytic activity of the partner. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:24728074 The peptide derived from Tyr(P)-534, a known c-Src kinase substrate, did not recruit SH2 domains from c-Src family kinases but did recruit PIK3R3 (C-terminal domain) and PLCG1 (NC tandem domain). |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: protein binding β undecided. Reason: The same PMID24728074 study uses SH2 and selected PTB domains, but the exact seeded partner/domain/phosphopeptide matrix entry has not been read. Do not copy a named SRC/PLCG/PIK3R result onto this distinct partner or assume every screened protein used the same domain. Preserve the experimental row as uncertain pending its table entry. |
| GO:0005515 protein binding | IPI PMID:24759320 Therapeutic targeting of BET bromodomain proteins in castrat... | KEEP AS NON CORE | Summary: protein binding β keep as non core. Reason: PMID24759320 explicitly reports BRD4 interaction with the AR N-terminal domain and receptor-regulatory effects. Retain the observed association as non-core while preserving the seeded BRD4-1 partner identity; the precise isoform/construct mapping and isolated coregulator interface have not been independently reconstructed. |
| GO:0005515 protein binding | IPI PMID:25091737 Identification of a new androgen receptor (AR) co-regulator ... | KEEP AS NON CORE | Summary: protein binding β keep as non core. Reason: PMID25091737 provides an AR ligand-binding-domain/BUD31 peptide structure and peptide effects on receptor activity. Retain that specific physical association without converting peptide antagonism into an established endogenous full-length BUD31 coactivator mechanism. |
| GO:0005515 protein binding | IPI PMID:26175416 DNA-PKcs-Mediated Transcriptional Regulation Drives Prostate... | MODIFY | Summary: protein binding β modify. Reason: The actual PMID26175416 AR-focused Results show ARβDNA-PKcs complex formation, persistence after ethidium bromide, AR-V7-containing complexes and receptor-dependent transcriptional function. Coactivator binding describes the measured association; it is not a claim that AR is a DNA-repair kinase or that the coimmunoprecipitate proves an isolated binary interface. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:26175416 AR and DNA-PKcs are found in complex PMID:26175416 DNA-PKcs is recruited with delayed kinetics to sites of AR function, and is required for maximum AR activity. |
| GO:0005515 protein binding | IPI PMID:27185910 Resistance to docetaxel in prostate cancer is associated wit... | MODIFY | Summary: KDM5D association supports enzyme binding. Reason: The complete own-paper abstract expressly states physical nuclear KDM5D-AR interaction and identifies KDM5D histone demethylation. Refine the partner class without attributing demethylation to AR. The other isoform-specific pair from this PMID is not closed by this general statement. Proposed replacements: enzyme binding Supporting Evidence: PMID:27185910 KDM5D physically interacts with AR in the nucleus |
| GO:0005515 protein binding | IPI PMID:27185910 Resistance to docetaxel in prostate cancer is associated wit... | UNDECIDED | Summary: protein binding β undecided. Reason: The generic KDM5DβAR association is supported, but the exact Q9BY66-3 partner mapping used for this separate row has not been resolved from the inspected abstract. Preserve this product-specific assertion and uncertainty rather than treating the unsuffixed record as proof of the same tested isoform. |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID33640491 uses human AR proximity labeling with separate confirmatory affinity purification. The exact seeded pairβs supplementary entry and confirmatory assay have not been inspected. Preserve the source-specific uncertainty; a known coregulator role from another paper does not change the meaning of this BioID assertion. |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID33640491 uses human AR proximity labeling with separate confirmatory affinity purification. The exact seeded pairβs supplementary entry and confirmatory assay have not been inspected. Preserve the source-specific uncertainty; a known coregulator role from another paper does not change the meaning of this BioID assertion. |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | MODIFY | Summary: KMT2A association supports histone methyltransferase binding. Reason: Actual cached Results explicitly confirm KMT2A after GFP-AR affinity purification in HEK293, beyond BioID proximity. Preserve that physical-association scope and identify the methyltransferase partner; no AR catalytic claim. Other source-specific BioID pairs remain unverified. Proposed replacements: histone methyltransferase binding Supporting Evidence: PMID:33640491 Using an affinity purification approach, we confirmed the previously reported association between AR and MED1 or KMT2A |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID33640491 uses human AR proximity labeling with separate confirmatory affinity purification. The exact seeded pairβs supplementary entry and confirmatory assay have not been inspected. Preserve the source-specific uncertainty; a known coregulator role from another paper does not change the meaning of this BioID assertion. |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID33640491 uses human AR proximity labeling with separate confirmatory affinity purification. The exact seeded pairβs supplementary entry and confirmatory assay have not been inspected. Preserve the source-specific uncertainty; a known coregulator role from another paper does not change the meaning of this BioID assertion. |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID33640491 uses human AR proximity labeling with separate confirmatory affinity purification. The exact seeded pairβs supplementary entry and confirmatory assay have not been inspected. Preserve the source-specific uncertainty; a known coregulator role from another paper does not change the meaning of this BioID assertion. |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID33640491 uses human AR proximity labeling with separate confirmatory affinity purification. The exact seeded pairβs supplementary entry and confirmatory assay have not been inspected. Preserve the source-specific uncertainty; a known coregulator role from another paper does not change the meaning of this BioID assertion. |
| GO:0005515 protein binding | IPI PMID:33640491 Proximity-dependent Mapping of the Androgen Receptor Identif... | UNDECIDED | Summary: protein binding β undecided. Reason: PMID33640491 uses human AR proximity labeling with separate confirmatory affinity purification. The exact seeded pairβs supplementary entry and confirmatory assay have not been inspected. Preserve the source-specific uncertainty; a known coregulator role from another paper does not change the meaning of this BioID assertion. |
| GO:0005634 nucleus | EXP PMID:12958311 The scaffolding protein RACK1 interacts with androgen recept... | ACCEPT | Summary: nucleus β accept. Reason: Retain the original experimentally supported nuclear receptor pool. The paper-specific ligand, splice-product and interaction contexts are preserved; nuclear localization is independently established across human AR studies and does not imply identical trafficking for every product. |
| GO:0005634 nucleus | EXP PMID:15634333 Androgen receptor function is modulated by the tissue-specif... | ACCEPT | Summary: nucleus β accept. Reason: Retain the original experimentally supported nuclear receptor pool. The paper-specific ligand, splice-product and interaction contexts are preserved; nuclear localization is independently established across human AR studies and does not imply identical trafficking for every product. |
| GO:0005634 nucleus | EXP PMID:17587566 PRMT2, a member of the protein arginine methyltransferase fa... | ACCEPT | Summary: nucleus β accept. Reason: Retain the original experimentally supported nuclear receptor pool. The paper-specific ligand, splice-product and interaction contexts are preserved; nuclear localization is independently established across human AR studies and does not imply identical trafficking for every product. Supporting Evidence: PMID:17587566 in the presence of androgens both proteins colocalize and translocate into the nucleus. |
| GO:0005634 nucleus | EXP PMID:19244107 A novel androgen receptor splice variant is up-regulated dur... | ACCEPT | Summary: nucleus β accept. Reason: Retain the original experimentally supported nuclear receptor pool. The paper-specific ligand, splice-product and interaction contexts are preserved; nuclear localization is independently established across human AR studies and does not imply identical trafficking for every product. |
| GO:0005634 nucleus | EXP PMID:25091737 Identification of a new androgen receptor (AR) co-regulator ... | ACCEPT | Summary: nucleus β accept. Reason: Retain the original experimentally supported nuclear receptor pool. The paper-specific ligand, splice-product and interaction contexts are preserved; nuclear localization is independently established across human AR studies and does not imply identical trafficking for every product. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: nucleus β accept. Reason: The PAINT nuclear location is strongly corroborated by human AR imaging and functional studies. Preserve the inherited PTN001182563 assertion, including legitimate target self-support, without claiming to have reconstructed the complete tree/MSA. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001182563 Β· PTN001182563 UNRESOLVED Original PAINT node retained; exact target-to-node topology/MSA not independently reconstructed. Target self-inclusion and donor count are not failure evidence; independent target biology is evaluated separately. |
| GO:0005634 nucleus | IDA PMID:15572661 Negative modulation of androgen receptor transcriptional act... | ACCEPT | Summary: nucleus β accept. Reason: Retain the original experimentally supported nuclear receptor pool. The paper-specific ligand, splice-product and interaction contexts are preserved; nuclear localization is independently established across human AR studies and does not imply identical trafficking for every product. |
| GO:0005634 nucleus | IDA PMID:19345326 Regulation of androgen receptor transcriptional activity and... | ACCEPT | Summary: nucleus β accept. Reason: Retain the original experimentally supported nuclear receptor pool. The paper-specific ligand, splice-product and interaction contexts are preserved; nuclear localization is independently established across human AR studies and does not imply identical trafficking for every product. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: nucleus β accept. Reason: The combined electronic nuclear-location assertion agrees with human AR experiments. Preserve its distinct domain, ortholog, UniProt and ARBA sources; broad corroboration is not a full rule audit. |
| GO:0005634 nucleus | IPI PMID:12612053 DJBP: a novel DJ-1-binding protein, negatively regulates the... | ACCEPT | Summary: nucleus β accept. Reason: Retain the original experimentally supported nuclear receptor pool. The paper-specific ligand, splice-product and interaction contexts are preserved; nuclear localization is independently established across human AR studies and does not imply identical trafficking for every product. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-376419 | ACCEPT | Summary: nucleoplasm β accept. Reason: The NRβMED1 event describes exchange of corepressor for mediator/coactivator complexes at target regulatory DNA. Its generic nuclear-receptor summary is not an AR-only assay; independently established AR chromatin occupancy supports the retained nucleoplasmic location. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-382096 | ACCEPT | Summary: nucleoplasm β accept. Reason: The NRβNCOR event represents receptor association with a transcriptional corepressor. Retain the nucleoplasmic receptor pool, supported independently by human AR repression studies, without treating the brief family-level summary as a new binary AR experiment. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4090390 | ACCEPT | Summary: nucleoplasm β accept. Reason: PIAS1/PIAS2 SUMOylate AR and reduce its transcriptional activation. The original nucleoplasmic location is retained for the regulated receptor substrate; SUMO ligase chemistry belongs to PIAS proteins. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5618080 | ACCEPT | Summary: nucleoplasm β accept. Reason: The HSP90/FKBP52 event describes receptor shuttling from the cytoplasm to the nucleus. Its detailed motor examples concern other steroid receptors; independent human AR translocation supports the same receptor pools without claiming every listed transport mechanism was directly tested for AR. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5618093 | ACCEPT | Summary: nucleoplasm β accept. Reason: HSP90 hydrolyses ATP and releases its ligand-bound receptor client. Reactome explicitly models the event in the nucleus but leaves transport-versus-dissociation timing uncertain. Retain the AR nucleoplasmic pool; do not attribute HSP90 ATPase activity to AR. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625738 | ACCEPT | Summary: nucleoplasm β accept. Reason: The activated PKN1βARβandrogen complex undergoes nuclear translocation. Retain the annotated receptor pool on the indicated side of this transport event, without assigning motor or kinase chemistry to AR. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625745 | ACCEPT | Summary: nucleoplasm β accept. Reason: PKN1 promotes formation of an ARβNCOA2 transcriptional complex. Retain the nucleoplasmic receptor location in coactivator recruitment. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625774 | ACCEPT | Summary: nucleoplasm β accept. Reason: The PKN1βAR complex associates with KLK2/KLK3 promoters. This target-promoter context supports the nucleoplasmic receptor pool. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625784 | ACCEPT | Summary: nucleoplasm β accept. Reason: PKN1 is recruited through AR at KLK2/KLK3 promoters and phosphorylates promoter-bound histone H3. Retain the nucleoplasmic receptor location; PKN1, rather than AR, performs phosphorylation. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625796 | ACCEPT | Summary: nucleoplasm β accept. Reason: KDM4C recruitment to methylated histone H3 follows PKN1-dependent promoter phosphorylation. Retain the curated AR nucleoplasmic pool in this target-promoter assembly, supported independently by ARβJMJD2C chromatin experiments; AR is not the methyl-lysine reader or demethylase. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625797 | ACCEPT | Summary: nucleoplasm β accept. Reason: KDM4C converts trimethylated histone H3 at KLK2/KLK3 promoters to the dimethylated state. AR is the promoter-associated receptor in the curated assembly; retain its nucleoplasmic location without assigning histone demethylation to AR. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625848 | ACCEPT | Summary: nucleoplasm β accept. Reason: KDM1A removes methylation from dimethylated histone H3 at AR-regulated promoters after the KDM4C step. Retain receptor nucleoplasmic localization; the reaction is catalysed by KDM1A. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625849 | ACCEPT | Summary: nucleoplasm β accept. Reason: PKN1-dependent histone phosphorylation permits recruitment of KDM1A to AR-regulated KLK2/KLK3 promoters. Retain the receptor location in the transcriptional assembly, distinct from KDM1A catalytic function. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5625870 | ACCEPT | Summary: nucleoplasm β accept. Reason: KDM1A removes the remaining monomethyl histone-H3 mark after the preceding dimethyl step at AR-regulated promoters. Retain AR nucleoplasmic localization, not a demethylase activity. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5696605 | ACCEPT | Summary: nucleoplasm β accept. Reason: USP12/WDR48/WDR20 and USP26 bind AR and promote its deubiquitination. Retain the curated nucleoplasmic receptor pool, with AR as the regulated substrate and the USPs as enzymes. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-8877902 | ACCEPT | Summary: nucleoplasm β accept. Reason: Ligand-activated AR forms a nuclear complex with RUNX2 and inhibits RUNX2 transcriptional activity. Retain the nucleoplasmic pool; the proposed TGF-beta/PSA extension is explicitly tentative in this event. |
| GO:0005737 cytoplasm | EXP PMID:12958311 The scaffolding protein RACK1 interacts with androgen recept... | ACCEPT | Summary: cytoplasm β accept. Reason: Retain the original cytoplasmic receptor pool in its experimental ligand/product context. Cytoplasmic residence before or during regulated nuclear entry is part of AR biology; it is not inconsistent with nuclear transcriptional function. |
| GO:0005737 cytoplasm | EXP PMID:17587566 PRMT2, a member of the protein arginine methyltransferase fa... | ACCEPT | Summary: cytoplasm β accept. Reason: Retain the original cytoplasmic receptor pool in its experimental ligand/product context. Cytoplasmic residence before or during regulated nuclear entry is part of AR biology; it is not inconsistent with nuclear transcriptional function. Supporting Evidence: PMID:17587566 Under androgen-free conditions, both AR and PRMT2 are confined to the cytoplasm |
| GO:0005737 cytoplasm | EXP PMID:19244107 A novel androgen receptor splice variant is up-regulated dur... | ACCEPT | Summary: cytoplasm β accept. Reason: Retain the original cytoplasmic receptor pool in its experimental ligand/product context. Cytoplasmic residence before or during regulated nuclear entry is part of AR biology; it is not inconsistent with nuclear transcriptional function. |
| GO:0005737 cytoplasm | IDA PMID:15572661 Negative modulation of androgen receptor transcriptional act... | ACCEPT | Summary: cytoplasm β accept. Reason: Retain the original cytoplasmic receptor pool in its experimental ligand/product context. Cytoplasmic residence before or during regulated nuclear entry is part of AR biology; it is not inconsistent with nuclear transcriptional function. |
| GO:0005737 cytoplasm | IDA PMID:17510388 DJ-1 binds androgen receptor directly and mediates its activ... | ACCEPT | Summary: cytoplasm β accept. Reason: Retain the original cytoplasmic receptor pool in its experimental ligand/product context. Cytoplasmic residence before or during regulated nuclear entry is part of AR biology; it is not inconsistent with nuclear transcriptional function. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: cytoplasm β accept. Reason: The electronic cytoplasm assignment is independently corroborated by human AR localization studies and the UniProt source note. Preserve the original donor/source fields without extrapolating identical distributions to all products. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: cytosol β accept. Reason: The live official Human Protein Atlas AR page directly reports supported cytosolic localization with antibody HPA004733. Retain the original IDA cellular pool; this does not claim universal absence from the nucleus or inspect image pixels. Supporting Evidence: file:human/AR/AR-notes.md The live [Human Protein Atlas AR subcellular page](https://www.proteinatlas.org/ENSG00000169083-AR/subcellular) reports supported cytosolic localization with antibody HPA004733. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5618080 | ACCEPT | Summary: cytosol β accept. Reason: The HSP90/FKBP52 event describes receptor shuttling from the cytoplasm to the nucleus. Its detailed motor examples concern other steroid receptors; independent human AR translocation supports the same receptor pools without claiming every listed transport mechanism was directly tested for AR. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5625717 | ACCEPT | Summary: cytosol β accept. Reason: Activated PKN1 binds androgen-activated AR in the curated cytosolic event. Retain this pre-import receptor pool; the kinase is PKN1. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5625738 | ACCEPT | Summary: cytosol β accept. Reason: The activated PKN1βARβandrogen complex undergoes nuclear translocation. Retain the annotated receptor pool on the indicated side of this transport event, without assigning motor or kinase chemistry to AR. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9705925 | ACCEPT | Summary: cytosol β accept. Reason: Androgens bind the AR ligand-binding domain while the receptor is an HSP90-complex client. Retain the ligand-responsive cytosolic pool; HSP90 supplies the chaperone ATPase cycle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9705926 | ACCEPT | Summary: cytosol β accept. Reason: The agonist-binding event concerns natural and synthetic ligands acting on AR. Retain the curated cytosolic receptor pool, independently corroborated by AR localization; the therapeutic examples are not additional AR molecular activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9706837 | ACCEPT | Summary: cytosol β accept. Reason: AR antagonist binding can block androgen binding, nuclear translocation and transcription. Retain the regulated cytosolic receptor pool; antagonist-induced retention does not imply absence from the nucleus in other conditions. |
| GO:0005886 plasma membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: plasma membrane β undecided. Reason: The exact mouse-derived plasma-membrane experiment and transfer scope remain unresolved. Intracellular trafficking and regulation of another proteinβs surface localization do not by themselves establish AR plasma-membrane residence. No biological impossibility is claimed. |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000002 | ACCEPT | Summary: regulation of DNA-templated transcription β accept. Reason: DNA-templated transcription regulation is a valid broad umbrella for the directly demonstrated receptor function. Retain the domain-derived IEA while distinguishing it from independent new process coverage. |
| GO:0007165 signal transduction | TAS PMID:10835690 Glucocorticoids can promote androgen-independent growth of p... | ACCEPT | Summary: signal transduction β accept. Reason: These broad signaling assertions are compatible with AR acting as an intercellular steroid-hormone receptor. PMID10835690 specifically studies a cortisol-responsive double-mutant AR in prostate cancer; that variant result is not generalized to wild-type cortisol specificity. Established normal androgen signaling independently corroborates the broad umbrella. Supporting Evidence: PMID:10835690 a doubly mutated AR functioned as a high-affinity cortisol/cortisone receptor |
| GO:0007267 cell-cell signaling | TAS PMID:10835690 Glucocorticoids can promote androgen-independent growth of p... | ACCEPT | Summary: cell-cell signaling β accept. Reason: These broad signaling assertions are compatible with AR acting as an intercellular steroid-hormone receptor. PMID10835690 specifically studies a cortisol-responsive double-mutant AR in prostate cancer; that variant result is not generalized to wild-type cortisol specificity. Established normal androgen signaling independently corroborates the broad umbrella. Supporting Evidence: PMID:10835690 a doubly mutated AR functioned as a high-affinity cortisol/cortisone receptor |
| GO:0007283 spermatogenesis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: spermatogenesis β keep as non core. Reason: Retain spermatogenesis as an established organismal consequence of AR signaling, secondary to the molecular receptor/transcription function. The PAINT node judgment is not challenged by the short donor list; exact topology remains unaudited. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002786997 Β· PTN002786997 UNRESOLVED Original PAINT node retained; exact target-to-node topology/MSA not independently reconstructed. Target self-inclusion and donor count are not failure evidence; independent target biology is evaluated separately. |
| GO:0008013 beta-catenin binding | IDA PMID:12799378 A direct beta-catenin-independent interaction between androg... | ACCEPT | Summary: beta-catenin binding β accept. Reason: PMID12799378 directly studies AR/beta-catenin/Tcf4 relationships, distinguishing ligand and bridging contexts. Retain beta-catenin binding as a specific receptor-coregulator interaction; this does not make AR a Wnt enzyme. |
| GO:0008013 beta-catenin binding | IPI PMID:12799378 A direct beta-catenin-independent interaction between androg... | ACCEPT | Summary: beta-catenin binding β accept. Reason: PMID12799378 directly studies AR/beta-catenin/Tcf4 relationships, distinguishing ligand and bridging contexts. Retain beta-catenin binding as a specific receptor-coregulator interaction; this does not make AR a Wnt enzyme. |
| GO:0008013 beta-catenin binding | TAS PMID:16344550 Differential use of functional domains by coiled-coil coacti... | ACCEPT | Summary: beta-catenin binding β accept. Reason: Retain the original TAS beta-catenin-binding assertion as supported by the cited synthesis and direct human AR/beta-catenin studies. Preserve the secondary citationβs evidence level rather than calling it a new direct assay. |
| GO:0008270 zinc ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: zinc ion binding β accept. Reason: The nuclear-receptor zinc-finger DNA-binding domain supports zinc binding as part of the receptor structure. Retain this electronic structural umbrella; no zinc transport or catalytic metal chemistry is asserted. |
| GO:0008284 positive regulation of cell population proliferation | IDA PMID:17277772 Cooperative demethylation by JMJD2C and LSD1 promotes androg... | KEEP AS NON CORE | Summary: positive regulation of cell population proliferation β keep as non core. Reason: PMID17277772 connects the receptor/cofactor transcriptional mechanism to prostate tumor-cell proliferation. Retain that positive growth effect as a context-specific outcome, not a separate universal core activity. |
| GO:0008285 negative regulation of cell population proliferation | IMP PMID:14521927 Androgen regulation of the human FERM domain encoding gene E... | KEEP AS NON CORE | Summary: negative regulation of cell population proliferation β keep as non core. Reason: PMID14521927 reports a context-dependent antiproliferative outcome. Opposite growth directions in different receptor/cell states are not by themselves contradictions; retain the original effect as secondary to transcriptional regulation. |
| GO:0008584 male gonad development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: male gonad development β keep as non core. Reason: Male gonad development is a physiological outcome of AR signaling. Retain the PAINT inference as non-core process context without treating donor count or species as evidence of failure. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002786997 Β· PTN002786997 UNRESOLVED Original PAINT node retained; exact target-to-node topology/MSA not independently reconstructed. Target self-inclusion and donor count are not failure evidence; independent target biology is evaluated separately. |
| GO:0010628 positive regulation of gene expression | IDA PMID:24681825 The NLR-related protein NWD1 is associated with prostate can... | ACCEPT | Summary: positive regulation of gene expression β accept. Reason: The original PMID24681825 source supports positive gene-expression regulation. Retain the broad process as an umbrella for ARβs direct transcriptional work, not an additional independent molecular function. |
| GO:0010628 positive regulation of gene expression | IMP PMID:14521927 Androgen regulation of the human FERM domain encoding gene E... | ACCEPT | Summary: positive regulation of gene expression β accept. Reason: The original PMID14521927 perturbation supports positive gene-expression regulation despite its distinct antiproliferative output. Retain this transcriptional umbrella and distinguish the downstream growth phenotype. |
| GO:0016607 nuclear speck | IDA PMID:23566155 Ski-interacting protein (SKIP) interacts with androgen recep... | KEEP AS NON CORE | Summary: nuclear speck β keep as non core. Reason: Actual PMID23566155 Results and Figure 5 describe tagged AR translocation/FRET at SKIP-positive speckle-like structures in BHK cells. Retain this specialized experimentally reported pool as non-core, with overexpression and compartment-identification limits; do not equate every AR focus with a native splicing speckle. Supporting Evidence: file:human/AR/AR-notes.md Tagged AR and SKIP interact at SKIP-positive speckle-like structures in BHK cells; prostate-cell reporter experiments are a separate model. |
| GO:0017053 transcription repressor complex | IPI PMID:18007036 Interaction between the androgen receptor and a segment of i... | KEEP AS NON CORE | Summary: transcription repressor complex β keep as non core. Reason: PMID18007036 directly resolves an AR ligand-binding-domain/SHP corepressor peptide complex. Retain the repressive-partner complex context as secondary, explicitly bounded to the tested fragments; the structure alone does not establish a constitutive endogenous holocomplex. |
| GO:0019899 enzyme binding | IEA GO_REF:0000107 | UNDECIDED | Summary: enzyme binding β undecided. Reason: The original mouse-derived enzyme-binding assertion lacks a resolved donor assay/partner in the inspected provenance. Other human AR enzyme associations do not identify this exact propagated claim; retain uncertainty without claiming enzyme contacts are absent. |
| GO:0019899 enzyme binding | IPI PMID:17277772 Cooperative demethylation by JMJD2C and LSD1 promotes androg... | MODIFY | Summary: enzyme binding β modify. Reason: PMID17277772 directly reports ARβJMJD2C interaction and coactivating chromatin function. Refine enzyme binding to coactivator binding in that same source, distinguishing the demethylaseβs chemistry from ARβs receptor role. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:17277772 JMJD2C interacts with androgen receptor in vitro and in vivo. PMID:17277772 Assembly of ligand-bound androgen receptor and JMJD2C on androgen receptor-target genes results in demethylation of trimethyl H3K9 and in stimulation of androgen receptor-dependent transcription. |
| GO:0019899 enzyme binding | IPI PMID:17587566 PRMT2, a member of the protein arginine methyltransferase fa... | MODIFY | Summary: enzyme binding β modify. Reason: PMID17587566 identifies PRMT2 as an AR-binding coactivator by interaction and functional assays. Refine to the measured coactivator-binding role rather than assigning methyltransferase activity to AR. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:17587566 a fragment of the AR was used in a library screen exploiting the yeast two-hybrid technique and identifying the C-terminal region of PRMT2. PMID:17587566 PRMT2 acts as a strong coactivator of the AR |
| GO:0030520 estrogen receptor signaling pathway | IDA PMID:10428808 Isolation and characterization of ARA160 as the first androg... | UNDECIDED | Summary: Estrogen-responsive AR reporters are established; assignment to this specific receptor pathway remains unresolved. Reason: The original PMID:10428808 Results and Figure 6 report estradiol-responsive wild-type AR reporters in PC-3 cells with ARA160 and DU145 cells with ARA70; these positive results are distinct from the E708K and T877A experiments. They support the separately retained cellular response to estrogen annotation. GO:0030520 describes a nuclear-receptor pathway initiated by estrogen binding and ending in a downstream cellular change. The measured reporter response in these transfected receptor/cofactor systems does not by itself resolve the initiating ligand-receptor mechanism or the intended pathway scope of this more specific annotation. The absence of ESR1/ESR2 names from the definition is therefore insufficient positive justification. Retain the original IDA evidence object but leave this pathway assignment unresolved; this is not a rejection of the observed wild-type response or a claim that AR cannot participate in estrogen signaling. Supporting Evidence: file:human/AR/AR-notes.md The actual Figure6 wild-type AR experiments show estradiol-responsive reporter activation in PC3 with ARA160 and in DU145 with ARA70; E708K and T877A were tested separately. |
| GO:0030521 androgen receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the PAINT androgen receptor signaling assertion as the direct central receptor pathway. The target-specific human evidence is extensive; the exact PTN002786997 topology was not reconstructed and donor count is not a weakness. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002786997 Β· PTN002786997 UNRESOLVED Original PAINT node retained; exact target-to-node topology/MSA not independently reconstructed. Target self-inclusion and donor count are not failure evidence; independent target biology is evaluated separately. |
| GO:0030521 androgen receptor signaling pathway | IDA PMID:10428808 Isolation and characterization of ARA160 as the first androg... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original direct-assay androgen receptor signaling annotation. The receptor performs ligand-responsive transcriptional work in the cited cellular/cofactor context; partner chemistry and downstream phenotypes remain separate. |
| GO:0030521 androgen receptor signaling pathway | IDA PMID:12799378 A direct beta-catenin-independent interaction between androg... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original direct-assay androgen receptor signaling annotation. The receptor performs ligand-responsive transcriptional work in the cited cellular/cofactor context; partner chemistry and downstream phenotypes remain separate. |
| GO:0030521 androgen receptor signaling pathway | IDA PMID:16120611 Modulation of androgen receptor transactivation by FoxH1. A ... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original direct-assay androgen receptor signaling annotation. The receptor performs ligand-responsive transcriptional work in the cited cellular/cofactor context; partner chemistry and downstream phenotypes remain separate. |
| GO:0030521 androgen receptor signaling pathway | IDA PMID:17277772 Cooperative demethylation by JMJD2C and LSD1 promotes androg... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original direct-assay androgen receptor signaling annotation. The receptor performs ligand-responsive transcriptional work in the cited cellular/cofactor context; partner chemistry and downstream phenotypes remain separate. |
| GO:0030521 androgen receptor signaling pathway | IDA PMID:19886863 Androgen regulation of the prostatic tumour suppressor NKX3.... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original direct-assay androgen receptor signaling annotation. The receptor performs ligand-responsive transcriptional work in the cited cellular/cofactor context; partner chemistry and downstream phenotypes remain separate. |
| GO:0030521 androgen receptor signaling pathway | IDA PMID:20048160 Androgen receptor-dependent transactivation of growth arrest... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original direct-assay androgen receptor signaling annotation. The receptor performs ligand-responsive transcriptional work in the cited cellular/cofactor context; partner chemistry and downstream phenotypes remain separate. |
| GO:0030521 androgen receptor signaling pathway | IDA PMID:20181722 TAF1 differentially enhances androgen receptor transcription... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original direct-assay androgen receptor signaling annotation. The receptor performs ligand-responsive transcriptional work in the cited cellular/cofactor context; partner chemistry and downstream phenotypes remain separate. |
| GO:0030521 androgen receptor signaling pathway | IDA PMID:21310825 The androgen receptor induces integrin Ξ±6Ξ²1 to promote prost... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original direct-assay androgen receptor signaling annotation. The receptor performs ligand-responsive transcriptional work in the cited cellular/cofactor context; partner chemistry and downstream phenotypes remain separate. |
| GO:0030521 androgen receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: The combined ARBA/InterPro androgen receptor pathway assignment is independently established on human AR. Preserve the electronic provenance without claiming the exact rule conditions were fully audited. |
| GO:0030521 androgen receptor signaling pathway | NAS PMID:12612053 DJBP: a novel DJ-1-binding protein, negatively regulates the... | ACCEPT | Summary: androgen receptor signaling pathway β accept. Reason: Retain the original NAS central androgen receptor pathway assertion. Its secondary evidence level remains unchanged, with direct human receptor studies providing independent corroboration. |
| GO:0030522 intracellular receptor signaling pathway | IDA PMID:17277772 Cooperative demethylation by JMJD2C and LSD1 promotes androg... | ACCEPT | Summary: intracellular receptor signaling pathway β accept. Reason: Intracellular receptor signaling is the valid parent process of AR-mediated steroid signaling. Retain the broad source assertion as a core umbrella, not redundant new coverage. |
| GO:0032991 protein-containing complex | IDA PMID:18468998 Blood pressure is regulated by an alpha1D-adrenergic recepto... | REMOVE | Summary: protein-containing complex β remove. Reason: The actual PMID18468998 construct/TAP-purification Methods, complete Table 3 and signalosome Results identify human alpha1 adrenergic receptor constructs and their syntrophin/dystrophin partners, not androgen receptor. An independent reviewer read those same target-defining sections and the GO0032991 definition. Remove this source-specific misattributed assertion; this is not inferred from title/acronym or a claim that AR never forms complexes. Supporting Evidence: file:human/AR/AR-notes.md Subsequent targeted reading resolved the construct/TAP-purification methods, the complete Table 3 participant inventory and Figures 4β5. Those assays explicitly use adrenergic receptor constructs and identify their associated proteins; androgen receptor is not among the reported table participants. |
| GO:0033574 response to testosterone | IEA GO_REF:0000117 | ACCEPT | Summary: response to testosterone β accept. Reason: The ARBA testosterone-response assignment is independently established for human full-length AR. Retain the original rule assertion; ligand-independent truncated products remain explicitly distinct. |
| GO:0033574 response to testosterone | NAS PMID:12612053 DJBP: a novel DJ-1-binding protein, negatively regulates the... | ACCEPT | Summary: response to testosterone β accept. Reason: Retain the original NAS testosterone-response context as consistent with established AR ligand signaling. Do not relabel the secondary source as a newly performed assay. |
| GO:0034056 estrogen response element binding | IBA GO_REF:0000033 | UNDECIDED | Summary: estrogen response element binding β undecided. Reason: The exact GO0034056 IBD at PTN001182563 is present in the local PAINT export, but target-to-node topology/MSA and the intended response-element assay scope remain unresolved. Human AR preference for AREs does not prove inability to bind every ERE. Neither donor count nor absence of target from a donor list rebuts the ancestral judgment. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN001182563 Β· PTN001182563 UNRESOLVED Exact local ERE IBD assertion inspected; full target-to-node topology/MSA and assay context remain unresolved. Target self-inclusion and donor count are not failure evidence; independent target biology is evaluated separately. Supporting Evidence: file:human/AR/AR-notes.md For estrogen response element binding, the local PAINT export contains the exact GO:0034056 IBD at PTN001182563. The target-to-node tree topology and MSA have not been reconstructed. |
| GO:0043565 sequence-specific DNA binding | IEA GO_REF:0000120 | ACCEPT | Summary: sequence-specific DNA binding β accept. Reason: Sequence-specific DNA recognition is directly established for human AR and coherent with the domain/ortholog assignment. Retain the broad electronic umbrella without changing its original provenance. |
| GO:0045597 positive regulation of cell differentiation | IMP PMID:14521927 Androgen regulation of the human FERM domain encoding gene E... | KEEP AS NON CORE | Summary: positive regulation of cell differentiation β keep as non core. Reason: The PMID14521927 differentiation phenotype is a context-specific downstream output of receptor transcription. Retain the original perturbation result as non-core rather than infer a separate direct differentiation catalyst. |
| GO:0045726 positive regulation of integrin biosynthetic process | IDA PMID:21310825 The androgen receptor induces integrin Ξ±6Ξ²1 to promote prost... | KEEP AS NON CORE | Summary: positive regulation of integrin biosynthetic process β keep as non core. Reason: PMID21310825 reports regulation of integrin production in its AR-expressing cell context. Retain the targeted regulatory outcome as secondary to the core transcription factor function; no new process is added. |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:11477070 DJ-1 positively regulates the androgen receptor by impairing... | ACCEPT | Summary: positive regulation of DNA-templated transcription β accept. Reason: The original PMID11477070 source measures positive receptor transcriptional activity in a coregulator context. Retain this broad transcriptional umbrella. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: The PAINT positive Pol II transcription assertion is directly corroborated on AR, including legitimate self-descendant experimental support. Retain the inherited core activity; exact topology remains unaudited rather than declared circular. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002786997 Β· PTN002786997 UNRESOLVED Original PAINT node retained; exact target-to-node topology/MSA not independently reconstructed. Target self-inclusion and donor count are not failure evidence; independent target biology is evaluated separately. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:12799378 A direct beta-catenin-independent interaction between androg... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: Retain the original source-specific positive Pol II transcription assertion. AR performs sequence-specific transcriptional regulation in the tested ligand/coregulator/cellular context; perturbation evidence is not confused with a partner enzyme activity. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:15572661 Negative modulation of androgen receptor transcriptional act... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: Retain the original source-specific positive Pol II transcription assertion. AR performs sequence-specific transcriptional regulation in the tested ligand/coregulator/cellular context; perturbation evidence is not confused with a partner enzyme activity. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:16728402 Glucocorticoid and androgen activation of monoamine oxidase ... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: Retain the original source-specific positive Pol II transcription assertion. AR performs sequence-specific transcriptional regulation in the tested ligand/coregulator/cellular context; perturbation evidence is not confused with a partner enzyme activity. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:17277772 Cooperative demethylation by JMJD2C and LSD1 promotes androg... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: Retain the original source-specific positive Pol II transcription assertion. AR performs sequence-specific transcriptional regulation in the tested ligand/coregulator/cellular context; perturbation evidence is not confused with a partner enzyme activity. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:17505061 Sirtuin 1 is required for antagonist-induced transcriptional... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: Retain the original source-specific positive Pol II transcription assertion. AR performs sequence-specific transcriptional regulation in the tested ligand/coregulator/cellular context; perturbation evidence is not confused with a partner enzyme activity. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:20048160 Androgen receptor-dependent transactivation of growth arrest... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: Retain the original source-specific positive Pol II transcription assertion. AR performs sequence-specific transcriptional regulation in the tested ligand/coregulator/cellular context; perturbation evidence is not confused with a partner enzyme activity. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:20181722 TAF1 differentially enhances androgen receptor transcription... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: Retain the original source-specific positive Pol II transcription assertion. AR performs sequence-specific transcriptional regulation in the tested ligand/coregulator/cellular context; perturbation evidence is not confused with a partner enzyme activity. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IMP PMID:19345326 Regulation of androgen receptor transcriptional activity and... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II β accept. Reason: Retain the original source-specific positive Pol II transcription assertion. AR performs sequence-specific transcriptional regulation in the tested ligand/coregulator/cellular context; perturbation evidence is not confused with a partner enzyme activity. |
| GO:0045945 positive regulation of transcription by RNA polymerase III | IDA PMID:18487222 Prohibitin and the SWI/SNF ATPase subunit BRG1 are required ... | UNDECIDED | Summary: positive regulation of transcription by RNA polymerase III β undecided. Reason: The inspected PMID18487222 experimental procedures and early/targeted Results explicitly expose polymerase II occupancy and PSA/KLK2 readouts. The distinct polymerase III experiment has not been located in a complete read of the paper. Preserve uncertainty rather than treating incomplete access or abstract silence as proof of overannotation. |
| GO:0051117 ATPase binding | IDA PMID:12058073 Novel ATPase of SNF2-like protein family interacts with andr... | ACCEPT | Summary: ATPase binding β accept. Reason: The original PMID12058073 ARIP4 study supports receptor binding to an ATPase regulatory partner. Retain the specific binding activity; the ATP hydrolysis/remodeling activity belongs to ARIP4, not AR. |
| GO:0060090 molecular adaptor activity | IDA PMID:11896058 Conformational analysis of the androgen receptor amino-termi... | UNDECIDED | Summary: molecular adaptor activity β undecided. Reason: PMID11896058βs inspected abstract establishes folding of an AR activation-domain fragment upon RAP74/TFIIF binding. The complete experiment establishing a simultaneous adaptor/bridging role has not been read. Retain the original IDA as uncertain rather than infer bridging from one interaction or replace it using unrelated cofactor papers. |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | IPI PMID:12799378 A direct beta-catenin-independent interaction between androg... | ACCEPT | Summary: RNA polymerase II-specific DNA-binding transcription factor binding β accept. Reason: PMID12799378 directly demonstrates AR DNA-binding-domain interaction with Tcf4 and its promoter/regulatory context. The specific transcription-factor-binding term captures the actual partner function. |
| GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding | IPI PMID:16120611 Modulation of androgen receptor transactivation by FoxH1. A ... | ACCEPT | Summary: RNA polymerase II-specific DNA-binding transcription factor binding β accept. Reason: PMID16120611 identifies FOXH1 interaction with AR. Retain the specific DNA-binding transcription-factor-binding term, distinct from assigning FOXH1βs transcriptional activity to AR. |
| GO:0070974 POU domain binding | IEA GO_REF:0000107 | UNDECIDED | Summary: POU domain binding β undecided. Reason: The exact mouse POU-domain binding experiment and donor-chain scope have not been resolved. General AR interactions with transcription factors cannot establish this particular domain specificity. Preserve the electronic assertion pending its evidence. |
| GO:0071383 cellular response to steroid hormone stimulus | IMP PMID:12902338 Identification of glucocorticoid receptor domains involved i... | ACCEPT | Summary: cellular response to steroid hormone stimulus β accept. Reason: Steroid-hormone responsiveness is a core receptor property in the cited perturbation context. Retain the broad cellular-response umbrella while distinguishing receptor variants and other receptors examined in the source. |
| GO:0071391 cellular response to estrogen stimulus | IDA PMID:10428808 Isolation and characterization of ARA160 as the first androg... | KEEP AS NON CORE | Summary: cellular response to estrogen stimulus β keep as non core. Reason: Actual PMID10428808 Figure6 and its Results show positive wild-type AR estradiol-responsive reporters in PC3 with ARA160 and DU145 with ARA70. E708K negative and T877A positive estradiol responses are separate experiments. Retain the original annotation as a secondary, transfected receptor/cofactor/cell context, without inferring a universal native estrogen response. This is a cellular response in the tested model, distinct from predominant physiological androgen signaling. Supporting Evidence: file:human/AR/AR-notes.md The actual Figure6 wild-type AR experiments show estradiol-responsive reporter activation in PC3 with ARA160 and in DU145 with ARA70; E708K and T877A were tested separately. |
| GO:0071394 cellular response to testosterone stimulus | IDA PMID:10428808 Isolation and characterization of ARA160 as the first androg... | ACCEPT | Summary: cellular response to testosterone stimulus β accept. Reason: Actual PMID10428808 assays measure testosterone-dependent receptor/coactivator activity. Retain the response as central to full-length AR function, with its tested cellular/construct context. |
| GO:0071394 cellular response to testosterone stimulus | IEA GO_REF:0000107 | ACCEPT | Summary: cellular response to testosterone stimulus β accept. Reason: The mouse-derived testosterone-response IEA is independently corroborated by direct human AR experiments. Preserve the original transfer provenance without asserting all receptor products require hormone. |
| GO:0140693 molecular condensate scaffold activity | IDA PMID:33978290 Low amounts of heavy water increase the phase separation pro... | ACCEPT | Summary: molecular condensate scaffold activity β accept. Reason: The complete PMID33978290 main text directly measures condensation of purified human AR activation-domain fragments under defined solution conditions. The official condensate-scaffold definition does not require heterotypic partners. Retain this molecular capacity with concentration/domain/in-vitro limits, not a blanket claim about all cellular puncta. Supporting Evidence: PMID:33978290 We observed that Tauβ5* indeed undergoes LLPS, as shown in Figure 1(b) , forming droplets capable of fusing |
| GO:0140693 molecular condensate scaffold activity | IDA PMID:36229685 Targeting androgen receptor phase separation to overcome ant... | ACCEPT | Summary: molecular condensate scaffold activity β accept. Reason: The PMID36229685 original abstract explicitly reports ligand-activated, transcriptionally active AR condensates and contributions from structured/unstructured domains. Retain the curated direct activity, distinguishing resistant variants; complete Methods/figure details remain uninspected and are not invented. Supporting Evidence: PMID:36229685 ligand-activated AR can form transcriptionally active condensates. |
| GO:0140694 membraneless organelle assembly | IDA PMID:36229685 Targeting androgen receptor phase separation to overcome ant... | ACCEPT | Summary: membraneless organelle assembly β accept. Reason: PMID36229685 directly reports AR condensate formation. AR supplies the assembling material, so this existing process represents its own structural work, not merely a requirement for another entityβs assembly. Retain with the same source-access and variant limits; no new process term is proposed. Supporting Evidence: PMID:36229685 Both structured and unstructured regions of AR contribute to the effective phase separation of AR and disordered N-terminal domain plays a predominant role. |
| GO:1902895 positive regulation of miRNA transcription | IDA PMID:25802280 Loss of Androgen-Regulated MicroRNA 1 Activates SRC and Prom... | ACCEPT | Summary: positive regulation of miRNA transcription β accept. Reason: The PMID25802280 miRNA-transcription assertion is a target-specific manifestation of ARβs direct transcriptional work. Retain the experimental process as core transcription context, without proposing redundant new ancestors/descendants. |
| GO:1903076 regulation of protein localization to plasma membrane | IDA PMID:21310825 The androgen receptor induces integrin Ξ±6Ξ²1 to promote prost... | KEEP AS NON CORE | Summary: regulation of protein localization to plasma membrane β keep as non core. Reason: The PMID21310825 surface-localization regulatory effect concerns the downstream targetβs trafficking, not automatic localization of AR itself to the plasma membrane. Retain the source-specific secondary process. |
| GO:1990837 sequence-specific double-stranded DNA binding | IEA GO_REF:0000117 | ACCEPT | Summary: sequence-specific double-stranded DNA binding β accept. Reason: The ARBA sequence-specific double-stranded DNA-binding assignment is independently established by AR response-element recognition. Retain this broad direct-function umbrella without claiming complete rule-condition reconstruction. |
| GO:2001237 negative regulation of extrinsic apoptotic signaling pathway | IDA PMID:21310825 The androgen receptor induces integrin Ξ±6Ξ²1 to promote prost... | KEEP AS NON CORE | Summary: negative regulation of extrinsic apoptotic signaling pathway β keep as non core. Reason: PMID21310825 reports a context-dependent reduction of extrinsic apoptotic signaling downstream of AR. Retain that physiological output as non-core; it does not make AR a death-receptor protease or justify a new apoptotic molecular activity. |
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Download this section (compressed HTML)Q: Which exact primary assay and PAINT ancestral placement support estrogen-response-element binding by human AR, beyond its established ARE preference?
Q: Does the PMID18487222 experiment establish RNA polymerase III transcriptional regulation, and does PMID11896058 demonstrate an adaptor bridge rather than pairwise TFIIF binding?
Q: Which SH2 phosphopeptide affinities are realized by endogenous full-length AR in defined ligand, phosphosite and cell states?
Q: How do ligand-binding-domain-deficient AR products and particular coregulators change condensate material properties and transcriptional output?
Experiment: Resolve the remaining source-specific partner tables and reagent identities before assigning a mechanism to the uncertain physical associations.
Experiment: Compare endogenous AR and defined splice products with matched ligand/phosphosite perturbations, chromatin occupancy and quantitative condensate measurements.
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