PHF23

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: Supported by UniProt localization data showing PHF23 is mainly present in the nucleus [PMID:25484098] Supporting Evidence: file:human/PHF23/PHF23-deep-research-falcon.md See deep research file for comprehensive analysis
GO:0031398 positive regulation of protein ubiquitination	IBA GO_REF:0000033	ACCEPT	Summary: Core function - PHF23 promotes ubiquitination and degradation of LRSAM1 [PMID:25484098]
GO:1901097 negative regulation of autophagosome maturation	IBA GO_REF:0000033	ACCEPT	Summary: Core function - PHF23 negatively regulates autophagy by promoting LRSAM1 degradation [PMID:25484098]
GO:1902902 negative regulation of autophagosome assembly	IBA GO_REF:0000033	ACCEPT	Summary: Core function - PHF23 overexpression impairs autophagy, knockdown enhances it [PMID:25484098]
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: Redundant with IBA annotation above but consistent; both support nuclear localization
GO:0005737 cytoplasm	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: PHF23 is partly localized in cytoplasm but cytosol (GO:0005829) is more specific; keep as non-core
GO:0006914 autophagy	IEA GO_REF:0000043	MODIFY	Summary: Too general - PHF23 is specifically a negative regulator of autophagy, not a general participant Proposed replacements: negative regulation of autophagy
GO:0008270 zinc ion binding	IEA GO_REF:0000043	ACCEPT	Summary: Supported - PHF23 contains a PHD-type zinc finger domain with Cys/His motif for Zn2+ coordination
GO:0046872 metal ion binding	IEA GO_REF:0000043	REMOVE	Summary: Redundant with more specific zinc ion binding annotation; zinc is the relevant metal
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: From high-throughput interactome mapping study - too generic, does not convey specific function Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
GO:0005654 nucleoplasm	IDA GO_REF:0000052	ACCEPT	Summary: Supported by immunofluorescence data showing nuclear localization; more specific than nucleus
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: PHF23 is partly localized in cytosol as per immunofluorescence data; supports interaction with LRSAM1
GO:0005515 protein binding	IPI PMID:25484098 PHF23 (plant homeodomain finger protein 23) negatively regul...	REMOVE	Summary: Reflects LRSAM1 interaction but protein binding is too generic; the functional consequence (ubiquitination regulation) is already annotated Supporting Evidence: PMID:25484098 PHF23 (plant homeodomain finger protein 23) negatively regulates cell autophagy by promoting ubiquitination and degradation of E3 ligase LRSAM1.
GO:0031398 positive regulation of protein ubiquitination	IMP PMID:25484098 PHF23 (plant homeodomain finger protein 23) negatively regul...	ACCEPT	Summary: Core function with direct experimental evidence - PHF23 promotes LRSAM1 ubiquitination and degradation Supporting Evidence: PMID:25484098 PHF23 (plant homeodomain finger protein 23) negatively regulates cell autophagy by promoting ubiquitination and degradation of E3 ligase LRSAM1.
GO:1901097 negative regulation of autophagosome maturation	IMP PMID:25484098 PHF23 (plant homeodomain finger protein 23) negatively regul...	ACCEPT	Summary: Core function - overexpression of PHF23 impairs autophagy with decreased LC3B-II levels Supporting Evidence: PMID:25484098 PHF23 (plant homeodomain finger protein 23) negatively regulates cell autophagy by promoting ubiquitination and degradation of E3 ligase LRSAM1.
GO:1902902 negative regulation of autophagosome assembly	IMP PMID:25484098 PHF23 (plant homeodomain finger protein 23) negatively regul...	ACCEPT	Summary: Core function - knockdown of PHF23 enhances autophagy, overexpression impairs it Supporting Evidence: PMID:25484098 PHF23 (plant homeodomain finger protein 23) negatively regulates cell autophagy by promoting ubiquitination and degradation of E3 ligase LRSAM1.