ASB9

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005515 protein binding	IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in...	REMOVE	Summary: Protein binding (IPI) with CKB. CKB is ASB9's best-characterized substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in...	REMOVE	Summary: Protein binding (IPI) with HIF1AN. HIF1AN is ASB9's most-replicated partner after CKB, recovered in several interactome screens. In human spermatogonial stem cells it co-immunoprecipitates with ASB9, and its re-expression reverses the effects of ASB9 overexpression, suggesting it is an ASB9 substrate, though its ubiquitination by ASB9 is not shown. Generic protein binding carries no functional information; removed under policy, with HIF1AN recorded as a candidate substrate. Reason: Removed under the generic protein-binding policy. The interaction is well replicated and functionally supported: [PMID:36683111 "Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency."] Supporting Evidence: PMID:36683111 Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency.
GO:0005515 protein binding	IPI PMID:19060904 An empirical framework for binary interactome mapping.	REMOVE	Summary: Protein binding (IPI) with CKB. CKB is ASB9's best-characterized substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:19060904 An empirical framework for binary interactome mapping.	REMOVE	Summary: Protein binding (IPI) with HIF1AN. HIF1AN is ASB9's most-replicated partner after CKB, recovered in several interactome screens. In human spermatogonial stem cells it co-immunoprecipitates with ASB9, and its re-expression reverses the effects of ASB9 overexpression, suggesting it is an ASB9 substrate, though its ubiquitination by ASB9 is not shown. Generic protein binding carries no functional information; removed under policy, with HIF1AN recorded as a candidate substrate. Reason: Removed under the generic protein-binding policy. The interaction is well replicated and functionally supported: [PMID:36683111 "Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency."] Supporting Evidence: PMID:36683111 Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency.
GO:0005515 protein binding	IPI PMID:20211142 An atlas of combinatorial transcriptional regulation in mous...	REMOVE	Summary: Protein binding (IPI) with ELOC. Elongin C is part of the CRL5(ASB9) complex, captured by the complex rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:21516116 Next-generation sequencing to generate interactome datasets.	REMOVE	Summary: Protein binding (IPI) with CKM. CKM is a creatine kinase, ASB9's substrate class. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Protein binding (IPI) with CKM. CKM is a creatine kinase, ASB9's substrate class. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Protein binding (IPI) with CKB. CKB is ASB9's best-characterized substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: Protein binding (IPI) with HEL-S-29. HEL-S-29 is an unreviewed creatine kinase B entry. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo...	REMOVE	Summary: Protein binding (IPI) with CRK. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	REMOVE	Summary: Protein binding (IPI) with CKM. CKM is a creatine kinase, ASB9's substrate class. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	REMOVE	Summary: Protein binding (IPI) with CKB. CKB is ASB9's best-characterized substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	REMOVE	Summary: Protein binding (IPI) with ELOC. Elongin C is part of the CRL5(ASB9) complex, captured by the complex rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	REMOVE	Summary: Protein binding (IPI) with HIF1AN. HIF1AN is ASB9's most-replicated partner after CKB, recovered in several interactome screens. In human spermatogonial stem cells it co-immunoprecipitates with ASB9, and its re-expression reverses the effects of ASB9 overexpression, suggesting it is an ASB9 substrate, though its ubiquitination by ASB9 is not shown. Generic protein binding carries no functional information; removed under policy, with HIF1AN recorded as a candidate substrate. Reason: Removed under the generic protein-binding policy. The interaction is well replicated and functionally supported: [PMID:36683111 "Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency."] Supporting Evidence: PMID:36683111 Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency.
GO:0005515 protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	REMOVE	Summary: Protein binding (IPI) with HIF1AN. HIF1AN is ASB9's most-replicated partner after CKB, recovered in several interactome screens. In human spermatogonial stem cells it co-immunoprecipitates with ASB9, and its re-expression reverses the effects of ASB9 overexpression, suggesting it is an ASB9 substrate, though its ubiquitination by ASB9 is not shown. Generic protein binding carries no functional information; removed under policy, with HIF1AN recorded as a candidate substrate. Reason: Removed under the generic protein-binding policy. The interaction is well replicated and functionally supported: [PMID:36683111 "Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency."] Supporting Evidence: PMID:36683111 Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding (IPI) with LCK. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding (IPI) with CKM. CKM is a creatine kinase, ASB9's substrate class. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding (IPI) with CKB. CKB is ASB9's best-characterized substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding (IPI) with CKMT1B. Mitochondrial creatine kinase is an ASB9 substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding (IPI) with ACTN3. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding (IPI) with ASB13. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding (IPI) with RELA. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein binding (IPI) with EXOSC1. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with DMWD. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with PRKN. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with KIF1B. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with LMNA. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with HSPA2. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with FKBP1A. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with TARDBP. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with SMN2. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	REMOVE	Summary: Protein binding (IPI) with JPH3. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Protein binding (IPI) with CKM. CKM is a creatine kinase, ASB9's substrate class. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Protein binding (IPI) with CKB. CKB is ASB9's best-characterized substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Protein binding (IPI) with CKMT1B. Mitochondrial creatine kinase is an ASB9 substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Protein binding (IPI) with ELOC. Elongin C is part of the CRL5(ASB9) complex, captured by the complex rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Protein binding (IPI) with HIF1AN. HIF1AN is ASB9's most-replicated partner after CKB, recovered in several interactome screens. In human spermatogonial stem cells it co-immunoprecipitates with ASB9, and its re-expression reverses the effects of ASB9 overexpression, suggesting it is an ASB9 substrate, though its ubiquitination by ASB9 is not shown. Generic protein binding carries no functional information; removed under policy, with HIF1AN recorded as a candidate substrate. Reason: Removed under the generic protein-binding policy. The interaction is well replicated and functionally supported: [PMID:36683111 "Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency."] Supporting Evidence: PMID:36683111 Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: Protein binding (IPI) with CKB. CKB is ASB9's best-characterized substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: Protein binding (IPI) with CKMT1B. Mitochondrial creatine kinase is an ASB9 substrate, captured by the adaptor and catabolism rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: Protein binding (IPI) with ELOC. Elongin C is part of the CRL5(ASB9) complex, captured by the complex rows. Generic protein binding carries no functional information; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: Protein binding (IPI) with HIF1AN. HIF1AN is ASB9's most-replicated partner after CKB, recovered in several interactome screens. In human spermatogonial stem cells it co-immunoprecipitates with ASB9, and its re-expression reverses the effects of ASB9 overexpression, suggesting it is an ASB9 substrate, though its ubiquitination by ASB9 is not shown. Generic protein binding carries no functional information; removed under policy, with HIF1AN recorded as a candidate substrate. Reason: Removed under the generic protein-binding policy. The interaction is well replicated and functionally supported: [PMID:36683111 "Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency."] Supporting Evidence: PMID:36683111 Based on the results of protein co-immunoprecipitation, HIF1AN had direct interaction with ASB9, and re-expression of HIF1AN partially restored the cell proliferation and apoptotic changes caused by ASB9 deficiency.
GO:0005739 mitochondrion	EXP PMID:20302626 ASB9 interacts with ubiquitous mitochondrial creatine kinase...	ACCEPT	Summary: Mitochondrion (EXP). ASB9 colocalizes with ubiquitous mitochondrial creatine kinase in mitochondria and induces its ubiquitination. Accepted. Reason: [PMID:20302626 "ASB9 and ASB9DeltaSOCS can interact and colocalise with uMtCK in the mitochondria."] [PMID:20302626 "The overexpression of ASB9, but not ASB9DeltaSOCS, induces ubiquitination of uMtCK."] Supporting Evidence: PMID:20302626 ASB9 and ASB9DeltaSOCS can interact and colocalise with uMtCK in the mitochondria. PMID:20302626 The overexpression of ASB9, but not ASB9DeltaSOCS, induces ubiquitination of uMtCK.
GO:0005739 mitochondrion	IEA GO_REF:0000044	ACCEPT	Summary: Mitochondrion (IEA). ASB9 colocalizes with ubiquitous mitochondrial creatine kinase in mitochondria and induces its ubiquitination. Accepted. Reason: Examined as a synthesis row (ORGANELLES batch 1). The mapping (GO_REF:0000044, SL-0173) comes from the UniProt location "Mitochondrion" with ECO:0000269 from PMID:20302626, the same study as the EXP row, so the feature the mapping assumes is really recorded and the organelle claim stands; the row matches the EXP row. No sub-compartment is added: ASB9 has no transit peptide or TM segment, the study used overexpressed protein, immunostaining and a crude 10,000 g mitochondrial pellet that resolve only the organelle, and the one location hint (its substrate uMtCK works in the intermembrane space at contact sites) is a single line that sits awkwardly with ASB9 acting as a cytosolic Cul5-RING substrate receptor. [PMID:20302626 "ASB9 and ASB9DeltaSOCS can interact and colocalise with uMtCK in the mitochondria."] [PMID:20302626 "The overexpression of ASB9, but not ASB9DeltaSOCS, induces ubiquitination of uMtCK."] Supporting Evidence: PMID:20302626 ASB9 and ASB9DeltaSOCS can interact and colocalise with uMtCK in the mitochondria. PMID:20302626 The overexpression of ASB9, but not ASB9DeltaSOCS, induces ubiquitination of uMtCK.
GO:0005829 cytosol	IEA GO_REF:0000117	ACCEPT	Summary: Cytosol (IEA, ARBA). ASB9 targets cytosolic creatine kinase B. Accepted. Reason: [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] Supporting Evidence: PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell.
GO:0005829 cytosol	TAS Reactome:R-HSA-8952039	ACCEPT	Summary: Cytosol (TAS, Reactome R-HSA-8952039: NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex). GOA derives this row from a cytosolic CRL5 reaction; the cached Reactome entry does not name ASB9. ASB9 targets cytosolic creatine kinase B. Accepted. Reason: [file:reactome/R-HSA-8952039.md "display_name: NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex"] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] Supporting Evidence: file:reactome/R-HSA-8952039.md display_name: NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell.
GO:0005829 cytosol	TAS Reactome:R-HSA-8952044	ACCEPT	Summary: Cytosol (TAS, Reactome R-HSA-8952044: AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex). GOA derives this row from a cytosolic CRL5 reaction; the cached Reactome entry does not name ASB9. ASB9 targets cytosolic creatine kinase B. Accepted. Reason: [file:reactome/R-HSA-8952044.md "display_name: AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex"] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] Supporting Evidence: file:reactome/R-HSA-8952044.md display_name: AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell.
GO:0005829 cytosol	TAS Reactome:R-HSA-8955241	ACCEPT	Summary: Cytosol (TAS, Reactome R-HSA-8955241: CAND1 binds cytosolic CRL E3 ubiquitin ligases). GOA derives this row from a cytosolic CRL5 reaction; the cached Reactome entry does not name ASB9. ASB9 targets cytosolic creatine kinase B. Accepted. Reason: [file:reactome/R-HSA-8955241.md "display_name: CAND1 binds cytosolic CRL E3 ubiquitin ligases"] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] Supporting Evidence: file:reactome/R-HSA-8955241.md display_name: CAND1 binds cytosolic CRL E3 ubiquitin ligases PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell.
GO:0005829 cytosol	TAS Reactome:R-HSA-8955289	ACCEPT	Summary: Cytosol (TAS, Reactome R-HSA-8955289: COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes). GOA derives this row from a cytosolic CRL5 reaction; the cached Reactome entry does not name ASB9. ASB9 targets cytosolic creatine kinase B. Accepted. Reason: [file:reactome/R-HSA-8955289.md "display_name: COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes"] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] Supporting Evidence: file:reactome/R-HSA-8955289.md display_name: COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell.
GO:0005829 cytosol	TAS Reactome:R-HSA-8956040	ACCEPT	Summary: Cytosol (TAS, Reactome R-HSA-8956040: COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes). GOA derives this row from a cytosolic CRL5 reaction; the cached Reactome entry does not name ASB9. ASB9 targets cytosolic creatine kinase B. Accepted. Reason: [file:reactome/R-HSA-8956040.md "display_name: COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes"] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] Supporting Evidence: file:reactome/R-HSA-8956040.md display_name: COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell.
GO:0016567 protein ubiquitination	IBA GO_REF:0000033	ACCEPT	Summary: Protein ubiquitination (IBA). ASB9 polyubiquitylates creatine kinases as the CRL5 substrate receptor. Core process. Reason: [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000651312 SUPPORTS TRANSFER ASB node seeded by ASB11 (UniProtKB:Q8WXH4) and by human ASB9 itself (UniProtKB:Q96DX5), which has its own experimental ubiquitination evidence. Supporting Evidence: PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell. PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB.
GO:0016567 protein ubiquitination	IDA PMID:17148442 Ankyrin repeat and suppressors of cytokine signaling box pro...	ACCEPT	Summary: Protein ubiquitination (IDA). ASB9 increases CKB polyubiquitylation, and the reconstituted ASB9-CUL5-RBX2 ligase ubiquitylates CKB in vitro. Core process. Reason: [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] Supporting Evidence: PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell. PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB.
GO:0016567 protein ubiquitination	IEA GO_REF:0000041	ACCEPT	Summary: Protein ubiquitination (IEA). ASB9 increases CKB polyubiquitylation, and the reconstituted ASB9-CUL5-RBX2 ligase ubiquitylates CKB in vitro. Core process. Reason: [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] Supporting Evidence: PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB. PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:23837592 Multimeric complexes among ankyrin-repeat and SOCS-box prote...	ACCEPT	Summary: Cul5-RING ubiquitin ligase complex (IDA). ASB9 forms a stable ternary complex with Elongin B/C that binds Cullin 5 (not Cullin 2), and the ASB9-CUL5-RBX2 ligase has been reconstituted and imaged by cryo-EM. Core complex. Reason: [PMID:23837592 "We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD."] [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] Supporting Evidence: PMID:23837592 We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD. PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:32513959 Structure and dynamics of the ASB9 CUL-RING E3 Ligase.	ACCEPT	Summary: Cul5-RING ubiquitin ligase complex (IDA). ASB9 forms a stable ternary complex with Elongin B/C that binds Cullin 5 (not Cullin 2), and the ASB9-CUL5-RBX2 ligase has been reconstituted and imaged by cryo-EM. Core complex. Reason: [PMID:32513959 "Here we report cryo-EM data for the substrate, creatine kinase (CKB) bound to ASB9-ELOB/C, and for full-length CUL5 bound to the RING protein, RBX2, which binds various E2s."] [PMID:23837592 "We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD."] [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] Supporting Evidence: PMID:32513959 Here we report cryo-EM data for the substrate, creatine kinase (CKB) bound to ASB9-ELOB/C, and for full-length CUL5 bound to the RING protein, RBX2, which binds various E2s. PMID:23837592 We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD. PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB.
GO:0031466 Cul5-RING ubiquitin ligase complex	IDA PMID:33268465 The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligas...	ACCEPT	Summary: Cul5-RING ubiquitin ligase complex (IDA). ASB9 forms a stable ternary complex with Elongin B/C that binds Cullin 5 (not Cullin 2), and the ASB9-CUL5-RBX2 ligase has been reconstituted and imaged by cryo-EM. Core complex. Reason: [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] [PMID:23837592 "We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD."] Supporting Evidence: PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB. PMID:23837592 We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD.
GO:0035556 intracellular signal transduction	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: Intracellular signal transduction (IEA, InterPro SOCS box). In ASB9 the SOCS box binds Elongin B/C to form the CRL5 ligase, and the signalling mapping is inherited from the cytokine-signalling SOCS proteins. ASB9 degrades metabolic enzymes (creatine kinases), with no signalling role. Marked as over-annotated, as in the SOCS4, ASB10 and ASB11 reviews. Reason: [PMID:23837592 "We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD."] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] Supporting Evidence: PMID:23837592 We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD. PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell.
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process	IDA PMID:25654263 How the ankyrin and SOCS box protein, ASB9, binds to creatin...	ACCEPT	Summary: Proteasome-mediated ubiquitin-dependent protein catabolic process (IDA). ASB9 targets creatine kinase for degradation, increasing CKB polyubiquitylation and lowering CKB levels in a SOCS box-dependent manner. In testis it degrades the transition protein TNP2. Core process. Reason: [PMID:25654263 "ASB9 binds to creatine kinase (CK) and targets it for degradation; however, the way in which ASB9 interacts with CK is not yet known."] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] [PMID:17148442 "The targeting of CKB for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme."] [PMID:41915740 "Mechanistically, we found that ASB9 assembles a testis-specific Cullin-RING ligase (CRL) complex-TNP2-ASB9-ELOB/C-CUL5-RBX1-that mediates the ubiquitin-dependent degradation of TNP2 to facilitate the histone-to-protamine transition during spermiogenesis."] Supporting Evidence: PMID:25654263 ASB9 binds to creatine kinase (CK) and targets it for degradation; however, the way in which ASB9 interacts with CK is not yet known. PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell. PMID:17148442 The targeting of CKB for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme. PMID:41915740 Mechanistically, we found that ASB9 assembles a testis-specific Cullin-RING ligase (CRL) complex-TNP2-ASB9-ELOB/C-CUL5-RBX1-that mediates the ubiquitin-dependent degradation of TNP2 to facilitate the histone-to-protamine transition during spermiogenesis.
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process	IDA PMID:33268465 The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligas...	ACCEPT	Summary: Proteasome-mediated ubiquitin-dependent protein catabolic process (IDA). ASB9 targets creatine kinase for degradation, increasing CKB polyubiquitylation and lowering CKB levels in a SOCS box-dependent manner. In testis it degrades the transition protein TNP2. Core process. Reason: [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] [PMID:17148442 "The targeting of CKB for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme."] [PMID:41915740 "Mechanistically, we found that ASB9 assembles a testis-specific Cullin-RING ligase (CRL) complex-TNP2-ASB9-ELOB/C-CUL5-RBX1-that mediates the ubiquitin-dependent degradation of TNP2 to facilitate the histone-to-protamine transition during spermiogenesis."] Supporting Evidence: PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB. PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell. PMID:17148442 The targeting of CKB for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme. PMID:41915740 Mechanistically, we found that ASB9 assembles a testis-specific Cullin-RING ligase (CRL) complex-TNP2-ASB9-ELOB/C-CUL5-RBX1-that mediates the ubiquitin-dependent degradation of TNP2 to facilitate the histone-to-protamine transition during spermiogenesis.
GO:0045732 positive regulation of protein catabolic process	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Positive regulation of protein catabolic process (IBA). ASB9 lowers CKB levels by targeting it for degradation. The term is correct in its outcome, but the core description of ASB9's role is direct participation in ubiquitin-dependent catabolism (GO:0043161, accepted); this regulation term is retained as a secondary, non-core description. Reason: [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] [PMID:17148442 "The targeting of CKB for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme."] Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000651312 SUPPORTS TRANSFER ASB node seeded by human ASB9 itself (UniProtKB:Q96DX5; IDA, PMID:17148442). Supporting Evidence: PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell. PMID:17148442 The targeting of CKB for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme.
GO:0045732 positive regulation of protein catabolic process	IDA PMID:17148442 Ankyrin repeat and suppressors of cytokine signaling box pro...	KEEP AS NON CORE	Summary: Positive regulation of protein catabolic process (IDA). ASB9 lowers CKB levels by targeting it for degradation. The term is correct in its outcome, but the core description of ASB9's role is direct participation in ubiquitin-dependent catabolism (GO:0043161, accepted); this regulation term is retained as a secondary, non-core description. Reason: [PMID:17148442 "This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell."] [PMID:17148442 "The targeting of CKB for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme."] Supporting Evidence: PMID:17148442 This interaction increases the polyubiquitylation of CKB and decreases total CKB levels within the cell. PMID:17148442 The targeting of CKB for degradation by Asb-9 was primarily SOCS box-dependent and suggests that Asb-9 acts as a specific ubiquitin ligase regulating levels of this evolutionarily conserved enzyme.
GO:1990756 ubiquitin-like ligase-substrate adaptor activity	IDA PMID:25654263 How the ankyrin and SOCS box protein, ASB9, binds to creatin...	ACCEPT	Summary: Ubiquitin-like ligase-substrate adaptor activity (IDA). ASB9 binds creatine kinase (one ASB9 per CK dimer) through its ankyrin repeats and recruits it to CUL5-RBX2 via its SOCS box-Elongin B/C module for ubiquitylation. Core function. Reason: [PMID:25654263 "ASB9 binds to creatine kinase (CK) and targets it for degradation; however, the way in which ASB9 interacts with CK is not yet known."] [PMID:25654263 "One ASB9 molecule binds to a dimer of CK."] [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] Supporting Evidence: PMID:25654263 ASB9 binds to creatine kinase (CK) and targets it for degradation; however, the way in which ASB9 interacts with CK is not yet known. PMID:25654263 One ASB9 molecule binds to a dimer of CK. PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB.
GO:1990756 ubiquitin-like ligase-substrate adaptor activity	IDA PMID:33268465 The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligas...	ACCEPT	Summary: Ubiquitin-like ligase-substrate adaptor activity (IDA). ASB9 binds creatine kinase (one ASB9 per CK dimer) through its ankyrin repeats and recruits it to CUL5-RBX2 via its SOCS box-Elongin B/C module for ubiquitylation. Core function. Reason: [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] [PMID:25654263 "One ASB9 molecule binds to a dimer of CK."] Supporting Evidence: PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB. PMID:25654263 One ASB9 molecule binds to a dimer of CK.
GO:1990756 ubiquitin-like ligase-substrate adaptor activity	IEA GO_REF:0000107	ACCEPT	Summary: Ubiquitin-like ligase-substrate adaptor activity (IEA). ASB9 binds creatine kinase (one ASB9 per CK dimer) through its ankyrin repeats and recruits it to CUL5-RBX2 via its SOCS box-Elongin B/C module for ubiquitylation. Core function. Reason: [PMID:25654263 "ASB9 binds to creatine kinase (CK) and targets it for degradation; however, the way in which ASB9 interacts with CK is not yet known."] [PMID:25654263 "One ASB9 molecule binds to a dimer of CK."] [PMID:33268465 "Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB."] Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q91ZT8 SUPPORTS TRANSFER Mouse Asb9; human ASB9 has its own IDA (PMID:25654263, PMID:33268465). Supporting Evidence: PMID:25654263 ASB9 binds to creatine kinase (CK) and targets it for degradation; however, the way in which ASB9 interacts with CK is not yet known. PMID:25654263 One ASB9 molecule binds to a dimer of CK. PMID:33268465 Here we have assembled and purified the Ankyrin repeat and SOCS Box protein 9 CUL5 RBX2 ligase (ASB9-CRL) in vitro and show how it ubiquitylates one of its substrates, CKB.
GO:0005634 nucleus	ISO PMID:41915740 ASB9 promotes ubiquitin-mediated degradation of TNP2 to faci...	NEW	Summary: Nucleus (NEW, ISO from mouse Asb9). In mouse spermatids, ASB9 appears in the nucleus from round-spermatid stages and is concentrated in the nuclei and perinuclear regions of elongating spermatids, where it degrades the chromatin protein TNP2. Reason: [PMID:41915740 "In mice, ASB9 showed weak expression in spermatogonia and spermatocytes, but initiating cytoplasmic and nuclear expression in round spermatids (steps 7 to 8)."] [PMID:41915740 "In contrast, ASB9 is mainly concentrated in the nuclei and perinuclear regions during steps 11 to 14, and becomes nearly undetectable by steps 15 to 16."] Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q91ZT8 SUPPORTS TRANSFER Mouse Asb9; spermatid nuclear immunostaining (PMID:41915740). The same study shows the TNP2 function in human patient sperm. Supporting Evidence: PMID:41915740 In mice, ASB9 showed weak expression in spermatogonia and spermatocytes, but initiating cytoplasmic and nuclear expression in round spermatids (steps 7 to 8). PMID:41915740 In contrast, ASB9 is mainly concentrated in the nuclei and perinuclear regions during steps 11 to 14, and becomes nearly undetectable by steps 15 to 16.
GO:0035092 sperm DNA condensation	IMP PMID:41915740 ASB9 promotes ubiquitin-mediated degradation of TNP2 to faci...	NEW	Summary: Sperm DNA condensation (NEW, IMP). ASB9 assembles a testis-specific CRL5 complex that ubiquitinates and degrades the transition protein TNP2. ASB9 deficiency in a patient and in knockout mice causes TNP2 retention, failure of the histone-to-protamine transition, sperm head malformation and male infertility. ASB9 performs the TNP2-removal step of the transition. Comparators: the E3 RNF8 and the proteasome activator PSME4 carry this term for the same chromatin-protein exchange. Reason: [PMID:41915740 "Mechanistically, we found that ASB9 assembles a testis-specific Cullin-RING ligase (CRL) complex-TNP2-ASB9-ELOB/C-CUL5-RBX1-that mediates the ubiquitin-dependent degradation of TNP2 to facilitate the histone-to-protamine transition during spermiogenesis."] [PMID:41915740 "In this study, we investigated the role of the ankyrin repeat-containing SOCS box protein 9 (ASB9) during spermiogenesis and found that its deficiency causes TNP2 retention, leading to a failure of the histone-to-protamine transition in both humans and mice."] [PMID:41915740 "This disruption consequently causes male infertility, characterized by sperm head malformation and impairments in fertilization and early embryonic development."] Supporting Evidence: PMID:41915740 Mechanistically, we found that ASB9 assembles a testis-specific Cullin-RING ligase (CRL) complex-TNP2-ASB9-ELOB/C-CUL5-RBX1-that mediates the ubiquitin-dependent degradation of TNP2 to facilitate the histone-to-protamine transition during spermiogenesis. PMID:41915740 In this study, we investigated the role of the ankyrin repeat-containing SOCS box protein 9 (ASB9) during spermiogenesis and found that its deficiency causes TNP2 retention, leading to a failure of the histone-to-protamine transition in both humans and mice. PMID:41915740 This disruption consequently causes male infertility, characterized by sperm head malformation and impairments in fertilization and early embryonic development.

Gene Description

Existing Annotations Review

Core Functions

Substrate receptor of the CRL5(ASB9) ligase that binds creatine kinases through its ankyrin repeats and targets CKB and mitochondrial creatine kinase for ubiquitination and degradation.

References

Suggested Questions for Experts

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Affinage

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