NCOA1 (SRC-1) is a p160-family nuclear transcriptional coactivator with bHLH/PAS domains, receptor-interaction motifs and activation regions that recruit additional cofactors. It potentiates steroid and other nuclear receptor transcription and can also cooperate with non-receptor transcription factors. Recruitment depends on receptor domains, ligands, promoter context and SRC1 splice isoform; androgen receptor AF1 contacts can differ from the classical LXXLLβAF2 interaction. SRC1 helps assemble chromatin-modifying and basal transcription machinery. Intrinsic histone H3/H4 acetyltransferase activity has been reported, although its physiological contribution relative to recruited acetyltransferases is less clear. Its endocrine, developmental and metabolic effects reflect tissue-specific transcriptional programs.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000435 obsolete positive regulation of transcription from RNA polymerase II promoter by galactose | IDA PMID:10207113 Molecular determinants of the estrogen receptor-coactivator ... | MODIFY | Summary: obsolete positive regulation of transcription from RNA polymerase II promoter by galactose: refine the functional claim. Reason: PMID:10207113: QuickGO confirms that the galactose-specific term is obsolete. The paper describes p160 recruitment by estrogen receptor. Refine to positive regulation of RNA polymerase II transcription, supported independently by SRC1 target experiments; the original GAL4/galactose assay-to-term mapping has not been reconstructed, and no physiological human galactose-response claim is inferred. Proposed replacements: positive regulation of transcription by RNA polymerase II Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0000785 chromatin | IDA PMID:15831516 Functional genomics identifies a mechanism for estrogen acti... | ACCEPT | Summary: chromatin: supported core claim. Reason: PMID:15831516: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0000785 chromatin | IDA PMID:17363140 The core component of the mammalian SWI/SNF complex SMARCD3/... | ACCEPT | Summary: chromatin: supported core claim. Reason: PMID:17363140: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:12628926 Here we report the purification and functional characterization of the human N-CoR complex. |
| GO:0000785 chromatin | ISA GO_REF:0000113 | ACCEPT | Summary: chromatin: supported core claim. Reason: GO_REF:0000113: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding | IEA GO_REF:0000107 | UNDECIDED | Summary: RNA polymerase II transcription regulatory region sequence-specific DNA binding: precise source claim remains unresolved. Reason: GO_REF:0000107: A p160 coactivator can occupy chromatin through a DNA-bound receptor, but occupancy does not itself establish direct or sequence-specific DNA binding. The exact ortholog source experiment behind this electronic transfer has not been resolved; retain uncertainty rather than infer absence of binding from its coactivator role. |
| GO:0003677 DNA binding | IEA GO_REF:0000107 | UNDECIDED | Summary: DNA binding: precise source claim remains unresolved. Reason: GO_REF:0000107: A p160 coactivator can occupy chromatin through a DNA-bound receptor, but occupancy does not itself establish direct or sequence-specific DNA binding. The exact ortholog source experiment behind this electronic transfer has not been resolved; retain uncertainty rather than infer absence of binding from its coactivator role. |
| GO:0003682 chromatin binding | IEA GO_REF:0000107 | UNDECIDED | Summary: chromatin binding: precise source claim remains unresolved. Reason: GO_REF:0000107: A p160 coactivator can occupy chromatin through a DNA-bound receptor, but occupancy does not itself establish direct or sequence-specific DNA binding. The exact ortholog source experiment behind this electronic transfer has not been resolved; retain uncertainty rather than infer absence of binding from its coactivator role. Supporting Evidence: PMID:17505061 Androgen antagonist-bound androgen receptor (AR) recruits SIRT1 and nuclear receptor corepressor to AR-responsive promoters |
| GO:0003712 transcription coregulator activity | TAS Reactome:R-HSA-5340251 | MODIFY | Summary: transcription coregulator activity: refine the functional claim. Reason: Reactome:R-HSA-5340251: Transcription coregulation is correct but the established positive coactivation mechanism supports the more informative existing transcription coactivator activity. Proposed replacements: transcription coactivator activity Supporting Evidence: PMID:17505061 Androgen antagonist-bound androgen receptor (AR) recruits SIRT1 and nuclear receptor corepressor to AR-responsive promoters |
| GO:0003713 transcription coactivator activity | IBA GO_REF:0000033 | ACCEPT | Summary: transcription coactivator activity: supported core claim. Reason: GO_REF:0000033: NCOA1 is a p160 transcriptional coactivator: it binds receptor activation domains and recruits additional transcription/chromatin cofactors. The original source is read together with independent target evidence; studies centered on another cofactor are not grounds to reject this established target function. Receptor, ligand, promoter and cell context determine the magnitude of coactivation. Supporting Evidence: PMID:17505061 Androgen antagonist-bound androgen receptor (AR) recruits SIRT1 and nuclear receptor corepressor to AR-responsive promoters |
| GO:0003713 transcription coactivator activity | IDA PMID:10207113 Molecular determinants of the estrogen receptor-coactivator ... | ACCEPT | Summary: transcription coactivator activity: supported core claim. Reason: PMID:10207113: NCOA1 is a p160 transcriptional coactivator: it binds receptor activation domains and recruits additional transcription/chromatin cofactors. The original source is read together with independent target evidence; studies centered on another cofactor are not grounds to reject this established target function. Receptor, ligand, promoter and cell context determine the magnitude of coactivation. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0003713 transcription coactivator activity | IDA PMID:15919756 Synovial sarcoma translocation (SYT) encodes a nuclear recep... | ACCEPT | Summary: transcription coactivator activity: supported core claim. Reason: PMID:15919756: NCOA1 is a p160 transcriptional coactivator: it binds receptor activation domains and recruits additional transcription/chromatin cofactors. The original source is read together with independent target evidence; studies centered on another cofactor are not grounds to reject this established target function. Receptor, ligand, promoter and cell context determine the magnitude of coactivation. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0003713 transcription coactivator activity | IDA PMID:17363140 The core component of the mammalian SWI/SNF complex SMARCD3/... | ACCEPT | Summary: transcription coactivator activity: supported core claim. Reason: PMID:17363140: NCOA1 is a p160 transcriptional coactivator: it binds receptor activation domains and recruits additional transcription/chromatin cofactors. The original source is read together with independent target evidence; studies centered on another cofactor are not grounds to reject this established target function. Receptor, ligand, promoter and cell context determine the magnitude of coactivation. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0003713 transcription coactivator activity | IEA GO_REF:0000120 | ACCEPT | Summary: transcription coactivator activity: supported core claim. Reason: GO_REF:0000120: NCOA1 is a p160 transcriptional coactivator: it binds receptor activation domains and recruits additional transcription/chromatin cofactors. The original source is read together with independent target evidence; studies centered on another cofactor are not grounds to reject this established target function. Receptor, ligand, promoter and cell context determine the magnitude of coactivation. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0003713 transcription coactivator activity | NAS PMID:15774904 Activation of ATP-binding cassette transporter A1 transcript... | ACCEPT | Summary: transcription coactivator activity: supported core claim. Reason: PMID:15774904: NCOA1 is a p160 transcriptional coactivator: it binds receptor activation domains and recruits additional transcription/chromatin cofactors. The original source is read together with independent target evidence; studies centered on another cofactor are not grounds to reject this established target function. Receptor, ligand, promoter and cell context determine the magnitude of coactivation. Supporting Evidence: PMID:12628926 Here we report the purification and functional characterization of the human N-CoR complex. |
| GO:0005515 protein binding | IPI PMID:10207113 Molecular determinants of the estrogen receptor-coactivator ... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:10207113: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0005515 protein binding | IPI PMID:11682626 Synergism between ERalpha transactivation function 1 (AF-1) ... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:11682626: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:11682626 Glutathione-S-transferase pulldown assays demonstrate that the AF-1 core is able and sufficient for the hERalpha N-terminal region to interact with SRC-1. |
| GO:0005515 protein binding | IPI PMID:12039952 Identification of protein arginine methyltransferase 2 as a ... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:12039952: The source directly identifies SRC1 association with an enzyme partner (PRMT2, UBE2L3 or TDG, respectively). Enzyme binding is more informative than bare protein binding and does not attribute the partner catalytic activity to SRC1. Proposed replacements: enzyme binding Supporting Evidence: PMID:12039952 PRMT2 was found to interact with two other coactivators, the steroid receptor coactivator-1 (SRC-1) |
| GO:0005515 protein binding | IPI PMID:12403843 A novel mutation in helix 12 of the vitamin D receptor impai... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:12403843: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:12403843 the mutant VDR had a marked impairment in binding steroid receptor coactivator 1 (SRC-1) |
| GO:0005515 protein binding | IPI PMID:12578355 2.1 A crystal structure of human PXR in complex with the St.... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:12578355: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:12917342 BAF60a mediates critical interactions between nuclear recept... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:12917342: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:14684751 The farnesoid X receptor controls gene expression in a ligan... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:14684751: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:14698205 In vitro farnesoid X receptor ligand sensor assay using surf... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:14698205: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:11486045 HERP uses its bHLH domain to recruit the mSin3 complex containing histone deacetylase HDAC1 and an additional corepressor, N-CoR, to mediate repression. |
| GO:0005515 protein binding | IPI PMID:15367689 The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:15367689: The source directly identifies SRC1 association with an enzyme partner (PRMT2, UBE2L3 or TDG, respectively). Enzyme binding is more informative than bare protein binding and does not attribute the partner catalytic activity to SRC1. Proposed replacements: enzyme binding Supporting Evidence: PMID:15367689 UBCH7 interacts with steroid receptor coactivator 1 (SRC-1) |
| GO:0005515 protein binding | IPI PMID:15641800 Induced alpha-helix structure in the aryl hydrocarbon recept... | REMOVE | Summary: protein binding: remove. Reason: PMID:15641800: The original paper directly maps TBL1/TBLR1 interactions with the N-CoR RD1/RD4 regions. Remove only the uninformative generic protein-binding annotation under current policy; the complex scaffold interaction remains documented. Supporting Evidence: PMID:12628926 TBL1/TBLR1 associates with N-CoR through two independent interactions: |
| GO:0005515 protein binding | IPI PMID:16282588 T:G mismatch-specific thymine-DNA glycosylase (TDG) as a cor... | REMOVE | Summary: protein binding: remove. Reason: PMID:16282588: The original paper directly maps TBL1/TBLR1 interactions with the N-CoR RD1/RD4 regions. Remove only the uninformative generic protein-binding annotation under current policy; the complex scaffold interaction remains documented. Supporting Evidence: PMID:12628926 TBL1/TBLR1 associates with N-CoR through two independent interactions: |
| GO:0005515 protein binding | IPI PMID:16282588 T:G mismatch-specific thymine-DNA glycosylase (TDG) as a cor... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:16282588: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:16282588 T:G mismatch-specific thymine-DNA glycosylase (TDG) as a cor... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:16282588: The source directly identifies SRC1 association with an enzyme partner (PRMT2, UBE2L3 or TDG, respectively). Enzyme binding is more informative than bare protein binding and does not attribute the partner catalytic activity to SRC1. Proposed replacements: enzyme binding Supporting Evidence: PMID:16282588 TDG interacts in vitro and in vivo with the p160 coactivator SRC1 |
| GO:0005515 protein binding | IPI PMID:16282588 T:G mismatch-specific thymine-DNA glycosylase (TDG) as a cor... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:16282588: The source directly identifies SRC1 association with an enzyme partner (PRMT2, UBE2L3 or TDG, respectively). Enzyme binding is more informative than bare protein binding and does not attribute the partner catalytic activity to SRC1. Proposed replacements: enzyme binding Supporting Evidence: PMID:16282588 TDG interacts in vitro and in vivo with the p160 coactivator SRC1 |
| GO:0005515 protein binding | IPI PMID:16456540 P38MAPK-dependent phosphorylation and degradation of SRC-3/A... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:16456540: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:16606617 Additional sex comb-like 1 (ASXL1), in cooperation with SRC-... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:16606617: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:16606617 Additional sex comb-like 1 (ASXL1), in cooperation with SRC-... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:16606617: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:16606617 Additional sex comb-like 1 (ASXL1), in cooperation with SRC-... | REMOVE | Summary: protein binding: remove uninformative generic binding. Reason: PMID:16606617: The source supports SRC1 association with another cofactor (ASXL1, GAS or ASC1). Under the current protein-binding policy, remove the uninformative generic GO:0005515 assertion when a better demonstrated molecular activity cannot be assigned from this pair. This does not deny the physical association. |
| GO:0005515 protein binding | IPI PMID:16957778 The catalytic subunit of the proteasome is engaged in the en... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:16957778: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:16957778 The catalytic subunit of the proteasome is engaged in the en... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:16957778: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:17254542 The vitamin D receptor interacts preferentially with DRIP205... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:17254542: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. Supporting Evidence: PMID:19955185 hPPARalpha SUMOylation on lysine 185 down-regulates its trans-activity through the selective recruitment of NCoR. |
| GO:0005515 protein binding | IPI PMID:17363140 The core component of the mammalian SWI/SNF complex SMARCD3/... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:17363140: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:17363140 The core component of the mammalian SWI/SNF complex SMARCD3/... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:17363140: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. Supporting Evidence: PMID:20581824 We report the crystal structure of a nuclear receptor-co-repressor (N-CoR) interaction domain 1 (ID1) peptide bound to truncated human Rev-erbalpha ligand-binding domain (LBD). |
| GO:0005515 protein binding | IPI PMID:17476305 SIP, a novel ankyrin repeat containing protein, sequesters s... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:17476305: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:17627277 PKA-induced resistance to tamoxifen is associated with an al... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:17627277: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:17627277 an altered orientation between ERalpha and its coactivator SRC-1 |
| GO:0005515 protein binding | IPI PMID:17641689 MED25 is distinct from TRAP220/MED1 in cooperating with CBP ... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:17641689: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:17673910 Structural and functional characterization of a novel type o... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:17673910: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:18391212 Identification of a potent synthetic FXR agonist with an une... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:18391212: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:19039327 GAS, a new glutamate-rich protein, interacts differentially ... | REMOVE | Summary: protein binding: remove uninformative generic binding. Reason: PMID:19039327: The source supports SRC1 association with another cofactor (ASXL1, GAS or ASC1). Under the current protein-binding policy, remove the uninformative generic GO:0005515 assertion when a better demonstrated molecular activity cannot be assigned from this pair. This does not deny the physical association. |
| GO:0005515 protein binding | IPI PMID:19786558 The basic helix-loop-helix proteins differentiated embryo ch... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:19786558: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:20203100 Structural basis for hydroxycholesterols as natural ligands ... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:20203100: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:20543827 A unique secondary-structure switch controls constitutive ge... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:20543827: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:20682316 Molecular determinants of the interactions between SRC-1 and... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:20682316: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:20682316 Molecular determinants of the interactions between SRC-1 and... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:20682316: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:20682316 the coactivator-binding surface of LXR, but not that of RXR, is critically important for physical and functional interactions with SRC-1 |
| GO:0005515 protein binding | IPI PMID:21454491 Repression of androgen receptor activity by HEYL, a third me... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:21454491: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:21478865 Common architecture of nuclear receptor heterodimers on DNA ... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:21478865: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:21478865 the binding of only one coactivator molecule per heterodimer, to RXR's partner. |
| GO:0005515 protein binding | IPI PMID:21478865 Common architecture of nuclear receptor heterodimers on DNA ... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:21478865: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:21478865 the binding of only one coactivator molecule per heterodimer, to RXR's partner. |
| GO:0005515 protein binding | IPI PMID:21478865 Common architecture of nuclear receptor heterodimers on DNA ... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:21478865: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:23602807 Structural and functional analysis of the human nuclear xeno... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:23602807: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:23602807 both PXR and RXRΞ± bind to the transcriptional coregulator SRC-1 with higher affinity when they are part of the PXR/RXRΞ± heterotetramer complex |
| GO:0005515 protein binding | IPI PMID:23602807 Structural and functional analysis of the human nuclear xeno... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:23602807: The cited receptor-coactivator study supports a nuclear receptor interaction. Nuclear receptor binding is the informative class already represented in this review; retain the exact original partner and source without assigning the receptor activity to SRC1. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:23602807 both PXR and RXRΞ± bind to the transcriptional coregulator SRC-1 with higher affinity when they are part of the PXR/RXRΞ± heterotetramer complex |
| GO:0005515 protein binding | IPI PMID:24907116 Identification and characterization of a ligand-selective mi... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:24907116: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:25219498 Modification of ASC1 by UFM1 is crucial for ERΞ± transactivat... | REMOVE | Summary: protein binding: remove uninformative generic binding. Reason: PMID:25219498: The source supports SRC1 association with another cofactor (ASXL1, GAS or ASC1). Under the current protein-binding policy, remove the uninformative generic GO:0005515 assertion when a better demonstrated molecular activity cannot be assigned from this pair. This does not deny the physical association. |
| GO:0005515 protein binding | IPI PMID:25962847 Tumor suppressor Menin acts as a corepressor of LXRΞ± to inhi... | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:25962847: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | UNDECIDED | Summary: protein binding: precise source claim remains unresolved. Reason: PMID:32296183: The original IPI assertion of protein binding is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0005515 protein binding | IPI PMID:9556555 Steroid receptor coactivator-1 interacts with the p50 subuni... | MODIFY | Summary: protein binding: refine the functional claim. Reason: PMID:9556555: The cited experiment identifies association with a DNA-binding transcription factor (AhR or NF-kappaB p50). Refine the bare binding assertion to the appropriate transcription-factor class. Proposed replacements: RNA polymerase II-specific DNA-binding transcription factor binding Supporting Evidence: PMID:9556555 Steroid receptor coactivator-1 (SRC-1) specifically bound to the transcription factor NFkappaB subunit p50 but not to p65 |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: nucleus: supported core claim. Reason: GO_REF:0000033: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: nucleus: supported core claim. Reason: GO_REF:0000120: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-400143 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-400143: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4085296 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-4085296: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5340251 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-5340251: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5579018 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-5579018: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9008270 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-9008270: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9023860 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-9023860: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9023884 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-9023884: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9029551 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-9029551: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9029561 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-9029561: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9029580 | ACCEPT | Summary: nucleoplasm: supported core claim. Reason: Reactome:R-HSA-9029580: Nuclear/chromatin recruitment is the normal setting for this transcriptional coactivator. The original location assertion agrees with receptor-dependent promoter recruitment and the curated nuclear localization; it does not imply sequence-specific DNA recognition by the coactivator. Supporting Evidence: PMID:15831516 ChIP assays showed that the coregulators SRC-1, SRC-3, and receptor-interacting protein 140 are recruited to this intronic module in an estrogen-dependent manner. |
| GO:0005667 transcription regulator complex | IEA GO_REF:0000117 | ACCEPT | Summary: transcription regulator complex: supported core claim. Reason: GO_REF:0000117: The protein participates in receptor-associated transcription regulatory complexes. These are context-dependent assemblies with receptors and additional cofactors, not a single obligatory stoichiometric complex shared by every promoter. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0005667 transcription regulator complex | IPI PMID:12909012 Coactivator binding promotes the specific interaction betwee... | ACCEPT | Summary: transcription regulator complex: supported core claim. Reason: PMID:12909012: The protein participates in receptor-associated transcription regulatory complexes. These are context-dependent assemblies with receptors and additional cofactors, not a single obligatory stoichiometric complex shared by every promoter. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0005667 transcription regulator complex | IPI PMID:20543827 A unique secondary-structure switch controls constitutive ge... | ACCEPT | Summary: transcription regulator complex: supported core claim. Reason: PMID:20543827: The protein participates in receptor-associated transcription regulatory complexes. These are context-dependent assemblies with receptors and additional cofactors, not a single obligatory stoichiometric complex shared by every promoter. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0005667 transcription regulator complex | IPI PMID:20682316 Molecular determinants of the interactions between SRC-1 and... | ACCEPT | Summary: transcription regulator complex: supported core claim. Reason: PMID:20682316: The protein participates in receptor-associated transcription regulatory complexes. These are context-dependent assemblies with receptors and additional cofactors, not a single obligatory stoichiometric complex shared by every promoter. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0006355 regulation of DNA-templated transcription | IEA GO_REF:0000002 | MODIFY | Summary: regulation of DNA-templated transcription: refine the functional claim. Reason: GO_REF:0000002: The general transcriptional regulation claim can be refined to positive regulation of transcription by RNA polymerase II, already supported by receptor reporter and recruitment experiments. Proposed replacements: positive regulation of transcription by RNA polymerase II Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0007595 lactation | IEA GO_REF:0000107 | UNDECIDED | Summary: lactation: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of lactation is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0008584 male gonad development | IEA GO_REF:0000107 | UNDECIDED | Summary: male gonad development: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of male gonad development is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0009725 response to hormone | IEA GO_REF:0000107 | MODIFY | Summary: response to hormone: refine the functional claim. Reason: GO_REF:0000107: The coactivator works inside the cell to mediate hormone-dependent transcription; cellular response to hormone stimulus is the supported existing refinement. Proposed replacements: cellular response to hormone stimulus Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0015721 bile acid and bile salt transport | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: bile acid and bile salt transport: pathway expansion exceeds the demonstrated work. Reason: GO_REF:0000117: The current GO definition describes directed movement of bile acids/salts by a transporter, pore or equivalent agent. The Reactome recycling pathway expands over regulatory machinery as well as transport. This nuclear coactivator regulates transporter expression through receptors; the cited pathway does not establish that it executes bile movement. Preserve the source assertion but flag the process mapping as overextended. |
| GO:0015721 bile acid and bile salt transport | TAS Reactome:R-HSA-159418 | MARK AS OVER ANNOTATED | Summary: bile acid and bile salt transport: pathway expansion exceeds the demonstrated work. Reason: Reactome:R-HSA-159418: The current GO definition describes directed movement of bile acids/salts by a transporter, pore or equivalent agent. The Reactome recycling pathway expands over regulatory machinery as well as transport. This nuclear coactivator regulates transporter expression through receptors; the cited pathway does not establish that it executes bile movement. Preserve the source assertion but flag the process mapping as overextended. |
| GO:0016922 nuclear receptor binding | IBA GO_REF:0000033 | ACCEPT | Summary: nuclear receptor binding: supported core claim. Reason: GO_REF:0000033: Binding nuclear receptors is integral to p160 coactivator recruitment. The target has direct receptor interaction evidence independent of the individual propagated assertion; receptor and motif preferences vary, and no universal requirement for this paralog is inferred. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0016922 nuclear receptor binding | IDA PMID:10207113 Molecular determinants of the estrogen receptor-coactivator ... | ACCEPT | Summary: nuclear receptor binding: supported core claim. Reason: PMID:10207113: Binding nuclear receptors is integral to p160 coactivator recruitment. The target has direct receptor interaction evidence independent of the individual propagated assertion; receptor and motif preferences vary, and no universal requirement for this paralog is inferred. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0016922 nuclear receptor binding | IEA GO_REF:0000120 | ACCEPT | Summary: nuclear receptor binding: supported core claim. Reason: GO_REF:0000120: Binding nuclear receptors is integral to p160 coactivator recruitment. The target has direct receptor interaction evidence independent of the individual propagated assertion; receptor and motif preferences vary, and no universal requirement for this paralog is inferred. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0016922 nuclear receptor binding | IPI PMID:17363140 The core component of the mammalian SWI/SNF complex SMARCD3/... | ACCEPT | Summary: nuclear receptor binding: supported core claim. Reason: PMID:17363140: Binding nuclear receptors is integral to p160 coactivator recruitment. The target has direct receptor interaction evidence independent of the individual propagated assertion; receptor and motif preferences vary, and no universal requirement for this paralog is inferred. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0016922 nuclear receptor binding | IPI PMID:18798693 Identification of COUP-TFII orphan nuclear receptor as a ret... | ACCEPT | Summary: nuclear receptor binding: supported core claim. Reason: PMID:18798693: Binding nuclear receptors is integral to p160 coactivator recruitment. The target has direct receptor interaction evidence independent of the individual propagated assertion; receptor and motif preferences vary, and no universal requirement for this paralog is inferred. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0021549 cerebellum development | IEA GO_REF:0000107 | UNDECIDED | Summary: cerebellum development: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of cerebellum development is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0021766 hippocampus development | IEA GO_REF:0000107 | UNDECIDED | Summary: hippocampus development: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of hippocampus development is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0021854 hypothalamus development | IEA GO_REF:0000107 | UNDECIDED | Summary: hypothalamus development: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of hypothalamus development is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0021987 cerebral cortex development | IEA GO_REF:0000107 | UNDECIDED | Summary: cerebral cortex development: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of cerebral cortex development is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0030331 obsolete nuclear estrogen receptor binding | IEA GO_REF:0000107 | MODIFY | Summary: obsolete nuclear estrogen receptor binding: refine the functional claim. Reason: GO_REF:0000107: QuickGO confirms that this receptor-subtype binding term is obsolete. Nuclear receptor binding preserves the supported interaction class; independent SRC1 receptor recruitment evidence supports the claim even where the particular source-specific comparator experiment remains unavailable. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:12628926 Here we report the purification and functional characterization of the human N-CoR complex. |
| GO:0030331 obsolete nuclear estrogen receptor binding | IPI PMID:18563714 ERAP75 functions as a coactivator to enhance estrogen recept... | MODIFY | Summary: obsolete nuclear estrogen receptor binding: refine the functional claim. Reason: PMID:18563714: QuickGO confirms that this receptor-subtype binding term is obsolete. Nuclear receptor binding preserves the supported interaction class; independent SRC1 receptor recruitment evidence supports the claim even where the particular source-specific comparator experiment remains unavailable. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0030520 estrogen receptor signaling pathway | IDA PMID:7481822 Sequence and characterization of a coactivator for the stero... | ACCEPT | Summary: estrogen receptor signaling pathway: supported core claim. Reason: PMID:7481822: SRC1 supplies coactivator work in receptor-dependent transcription, rather than acting as a passive hormone substrate. The steroid receptor studies support estrogen and progesterone pathway participation, with receptor isoform and promoter context affecting recruitment. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0032355 response to estradiol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to estradiol: supported contextual role. Reason: GO_REF:0000107: These specific hormone responses are compatible with documented estrogen/retinoid/progesterone receptor coactivation. Retain as receptor-context manifestations of a broader coactivator role, not evidence of exclusive hormone specificity. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). PMID:17363140 This coactivating property is dependent on SRC1 expression, showing that HATs and SWI/SNF cooperate in this retinoid-controlled transcriptional process. |
| GO:0032526 response to retinoic acid | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to retinoic acid: supported contextual role. Reason: GO_REF:0000107: These specific hormone responses are compatible with documented estrogen/retinoid/progesterone receptor coactivation. Retain as receptor-context manifestations of a broader coactivator role, not evidence of exclusive hormone specificity. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). PMID:17363140 This coactivating property is dependent on SRC1 expression, showing that HATs and SWI/SNF cooperate in this retinoid-controlled transcriptional process. |
| GO:0032570 response to progesterone | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to progesterone: supported contextual role. Reason: GO_REF:0000107: These specific hormone responses are compatible with documented estrogen/retinoid/progesterone receptor coactivation. Retain as receptor-context manifestations of a broader coactivator role, not evidence of exclusive hormone specificity. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). PMID:17363140 This coactivating property is dependent on SRC1 expression, showing that HATs and SWI/SNF cooperate in this retinoid-controlled transcriptional process. |
| GO:0032870 cellular response to hormone stimulus | IBA GO_REF:0000033 | ACCEPT | Summary: cellular response to hormone stimulus: supported core claim. Reason: GO_REF:0000033: Hormone-dependent recruitment of the coactivator directly changes transcriptional output. This is participation in cellular hormone response, not merely a change in coactivator expression. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0032870 cellular response to hormone stimulus | IEA GO_REF:0000107 | ACCEPT | Summary: cellular response to hormone stimulus: supported core claim. Reason: GO_REF:0000107: Hormone-dependent recruitment of the coactivator directly changes transcriptional output. This is participation in cellular hormone response, not merely a change in coactivator expression. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0032991 protein-containing complex | IMP PMID:15641800 Induced alpha-helix structure in the aryl hydrocarbon recept... | MODIFY | Summary: protein-containing complex: refine the functional claim. Reason: PMID:15641800: The source reports association with the aryl hydrocarbon receptor transcription machinery. The existing transcription regulator complex term is more informative than generic protein-containing complex. Proposed replacements: transcription regulator complex Supporting Evidence: PMID:15641800 In protein-protein interaction studies, the acidic Q-rich region bound to components of the general transcription machinery [TATA-binding protein (TBP), TAF4, and TAF6] as well as the coactivator proteins SRC-1a and TIF2. |
| GO:0035357 peroxisome proliferator activated receptor signaling pathway | NAS PMID:16373399 A novel partial agonist of peroxisome proliferator-activated... | UNDECIDED | Summary: peroxisome proliferator activated receptor signaling pathway: precise source claim remains unresolved. Reason: PMID:16373399: PMID16373399 describes PGC1alpha-preferential PPARgamma ligand responses in its abstract. The full target-specific SRC assay/physiological attribution is not accessible in the normal cache; this is not evidence of misattribution, because the full paper may assay additional cofactors. Do not convert a compound or partner phenotype into a core function of this protein. |
| GO:0042789 mRNA transcription by RNA polymerase II | IDA PMID:16373399 A novel partial agonist of peroxisome proliferator-activated... | MODIFY | Summary: mRNA transcription by RNA polymerase II: refine the functional claim. Reason: PMID:16373399: This cofactor stimulates RNA polymerase II transcription through transcription-factor recruitment; it is not the polymerase. Positive regulation of RNA polymerase II transcription states its contribution more accurately. Proposed replacements: positive regulation of transcription by RNA polymerase II Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0042974 obsolete nuclear retinoic acid receptor binding | IEA GO_REF:0000107 | MODIFY | Summary: obsolete nuclear retinoic acid receptor binding: refine the functional claim. Reason: GO_REF:0000107: QuickGO confirms that this receptor-subtype binding term is obsolete. Nuclear receptor binding preserves the supported interaction class; independent SRC1 receptor recruitment evidence supports the claim even where the particular source-specific comparator experiment remains unavailable. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0043065 positive regulation of apoptotic process | IEA GO_REF:0000107 | UNDECIDED | Summary: positive regulation of apoptotic process: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of positive regulation of apoptotic process is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0044849 estrous cycle | IEA GO_REF:0000107 | UNDECIDED | Summary: estrous cycle: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of estrous cycle is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | UNDECIDED | Summary: protein-containing complex binding: precise source claim remains unresolved. Reason: GO_REF:0000107: The broad interaction inference is plausible for a multidomain coactivator, but its specific dimer or complex-binding assay/source has not been resolved. Recruitment to a receptor complex does not alone specify the asserted molecular activity. |
| GO:0045666 positive regulation of neuron differentiation | IEA GO_REF:0000107 | UNDECIDED | Summary: positive regulation of neuron differentiation: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of positive regulation of neuron differentiation is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:11891224 Cross-repression, a functional consequence of the physical i... | MODIFY | Summary: positive regulation of DNA-templated transcription: refine the functional claim. Reason: PMID:11891224: The general transcriptional regulation claim can be refined to positive regulation of transcription by RNA polymerase II, already supported by receptor reporter and recruitment experiments. Proposed replacements: positive regulation of transcription by RNA polymerase II Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:15367689 The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator... | MODIFY | Summary: positive regulation of DNA-templated transcription: refine the functional claim. Reason: PMID:15367689: The general transcriptional regulation claim can be refined to positive regulation of transcription by RNA polymerase II, already supported by receptor reporter and recruitment experiments. Proposed replacements: positive regulation of transcription by RNA polymerase II Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0045925 positive regulation of female receptivity | IEA GO_REF:0000107 | UNDECIDED | Summary: positive regulation of female receptivity: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of positive regulation of female receptivity is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IBA GO_REF:0000033 | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II: supported core claim. Reason: GO_REF:0000033: Positive regulation of RNA polymerase II transcription is the principal consequence of receptor-bound coactivator recruitment. Target-specific coactivation studies support the claim collectively without making this cofactor indispensable for every nuclear receptor response. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:15919756 Synovial sarcoma translocation (SYT) encodes a nuclear recep... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II: supported core claim. Reason: PMID:15919756: Positive regulation of RNA polymerase II transcription is the principal consequence of receptor-bound coactivator recruitment. Target-specific coactivation studies support the claim collectively without making this cofactor indispensable for every nuclear receptor response. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:16373399 A novel partial agonist of peroxisome proliferator-activated... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II: supported core claim. Reason: PMID:16373399: Positive regulation of RNA polymerase II transcription is the principal consequence of receptor-bound coactivator recruitment. Target-specific coactivation studies support the claim collectively without making this cofactor indispensable for every nuclear receptor response. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:9223431 A splicing variant of Steroid Receptor Coactivator-1 (SRC-1E... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II: supported core claim. Reason: PMID:9223431: Positive regulation of RNA polymerase II transcription is the principal consequence of receptor-bound coactivator recruitment. Target-specific coactivation studies support the claim collectively without making this cofactor indispensable for every nuclear receptor response. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IEA GO_REF:0000120 | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II: supported core claim. Reason: GO_REF:0000120: Positive regulation of RNA polymerase II transcription is the principal consequence of receptor-bound coactivator recruitment. Target-specific coactivation studies support the claim collectively without making this cofactor indispensable for every nuclear receptor response. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0045944 positive regulation of transcription by RNA polymerase II | NAS PMID:12909012 Coactivator binding promotes the specific interaction betwee... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II: supported core claim. Reason: PMID:12909012: Positive regulation of RNA polymerase II transcription is the principal consequence of receptor-bound coactivator recruitment. Target-specific coactivation studies support the claim collectively without making this cofactor indispensable for every nuclear receptor response. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0045944 positive regulation of transcription by RNA polymerase II | NAS PMID:15774904 Activation of ATP-binding cassette transporter A1 transcript... | ACCEPT | Summary: positive regulation of transcription by RNA polymerase II: supported core claim. Reason: PMID:15774904: Positive regulation of RNA polymerase II transcription is the principal consequence of receptor-bound coactivator recruitment. Target-specific coactivation studies support the claim collectively without making this cofactor indispensable for every nuclear receptor response. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0046965 obsolete nuclear retinoid X receptor binding | IEA GO_REF:0000107 | MODIFY | Summary: obsolete nuclear retinoid X receptor binding: refine the functional claim. Reason: GO_REF:0000107: QuickGO confirms that this receptor-subtype binding term is obsolete. Nuclear receptor binding preserves the supported interaction class; independent SRC1 receptor recruitment evidence supports the claim even where the particular source-specific comparator experiment remains unavailable. Proposed replacements: nuclear receptor binding Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0046983 protein dimerization activity | IEA GO_REF:0000002 | UNDECIDED | Summary: protein dimerization activity: precise source claim remains unresolved. Reason: GO_REF:0000002: The broad interaction inference is plausible for a multidomain coactivator, but its specific dimer or complex-binding assay/source has not been resolved. Recruitment to a receptor complex does not alone specify the asserted molecular activity. |
| GO:0050847 progesterone receptor signaling pathway | IDA PMID:10757795 The opposing transcriptional activities of the two isoforms ... | ACCEPT | Summary: progesterone receptor signaling pathway: supported core claim. Reason: PMID:10757795: SRC1 supplies coactivator work in receptor-dependent transcription, rather than acting as a passive hormone substrate. The steroid receptor studies support estrogen and progesterone pathway participation, with receptor isoform and promoter context affecting recruitment. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:0060179 male mating behavior | IEA GO_REF:0000107 | UNDECIDED | Summary: male mating behavior: precise source claim remains unresolved. Reason: GO_REF:0000107: The original IEA assertion of male mating behavior is preserved. The available source material does not resolve the target-specific experiment or transfer supporting this precise claim; neither another gene in the title nor a family-level expectation establishes an error. Additional primary evidence is needed. |
| GO:0061733 protein-lysine-acetyltransferase activity | IEA GO_REF:0000120 | MODIFY | Summary: protein-lysine-acetyltransferase activity: refine the functional claim. Reason: GO_REF:0000120: Direct biochemical work reports intrinsic SRC1 acetyltransferase activity primarily toward histones H3 and H4. Refine the broad protein-lysine activity to histone acetyltransferase activity. Its quantitative contribution relative to recruited CBP/p300/PCAF in vivo remains unclear, so it is not elevated to a separate core mechanism. Proposed replacements: histone acetyltransferase activity Supporting Evidence: PMID:9296499 Here we show that SRC-1 possesses intrinsic histone acetyltransferase activity PMID:9296499 The HAT activity of SRC-1 maps to its carboxy-terminal region and is primarily specific for histones H3 and H4. |
| GO:0090575 RNA polymerase II transcription regulator complex | IDA PMID:16373399 A novel partial agonist of peroxisome proliferator-activated... | ACCEPT | Summary: RNA polymerase II transcription regulator complex: supported core claim. Reason: PMID:16373399: The protein participates in receptor-associated transcription regulatory complexes. These are context-dependent assemblies with receptors and additional cofactors, not a single obligatory stoichiometric complex shared by every promoter. Supporting Evidence: PMID:7481822 Because the protein stimulated transactivation of all the steroid receptors tested, it has been termed steroid receptor coactivator-1 (SRC-1). |
| GO:1900076 regulation of cellular response to insulin stimulus | NAS PMID:16373399 A novel partial agonist of peroxisome proliferator-activated... | UNDECIDED | Summary: regulation of cellular response to insulin stimulus: precise source claim remains unresolved. Reason: PMID:16373399: PMID16373399 describes PGC1alpha-preferential PPARgamma ligand responses in its abstract. The full target-specific SRC assay/physiological attribution is not accessible in the normal cache; this is not evidence of misattribution, because the full paper may assay additional cofactors. Do not convert a compound or partner phenotype into a core function of this protein. |
| GO:1904179 positive regulation of adipose tissue development | NAS PMID:16373399 A novel partial agonist of peroxisome proliferator-activated... | UNDECIDED | Summary: positive regulation of adipose tissue development: precise source claim remains unresolved. Reason: PMID:16373399: PMID16373399 describes PGC1alpha-preferential PPARgamma ligand responses in its abstract. The full target-specific SRC assay/physiological attribution is not accessible in the normal cache; this is not evidence of misattribution, because the full paper may assay additional cofactors. Do not convert a compound or partner phenotype into a core function of this protein. |
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