ASB10

Summary: The curated HuRI IPI annotation reports ASB10 binding to LCN2. Retain this supported association as non-core protein binding; no more specific ASB10 molecular function is established for this pair.

Reason: The preserved IntAct-derived GOA row identifies P80188, and the reviewed ASB10 UniProt record carries the same IntAct-derived partner edge with NbExp=3. This is pair-specific curated interaction metadata, not an independent source or proof of three independent physiological replications. The HuRI paper describes human ORF yeast two-hybrid screening, pairwise retesting and sequence confirmation. Its exact ASB10 target-table row, construct orientation and pair-specific orthogonal controls were not independently inspected; the study-level quote supports the screening protocol only. The association does not establish that LCN2 is an ASB10 ubiquitination substrate or that ASB10 has receptor or transporter activity. In the absence of contrary evidence or a supported finer molecular-function assignment, the source-specific association is retained under the standing project instruction for correct generic binding.

Summary: The curated HuRI IPI annotation reports ASB10 binding to MEOX2. Retain this supported association as non-core protein binding; no more specific ASB10 molecular function is established for this pair.

Reason: The preserved IntAct-derived GOA row identifies Q6FHY5, and the reviewed ASB10 UniProt record carries the same IntAct-derived partner edge with NbExp=3. This is pair-specific curated interaction metadata, not an independent source or proof of three independent physiological replications. The HuRI paper describes human ORF yeast two-hybrid screening, pairwise retesting and sequence confirmation. Its exact ASB10 target-table row, construct orientation and pair-specific orthogonal controls were not independently inspected; the study-level quote supports the screening protocol only. The association does not establish that MEOX2 is an ASB10 ubiquitination substrate or confer MEOX2 DNA-binding or transcriptional functions on ASB10. Transcription factor binding (GO:0008134) describes binding a transcription factor, so MEOX2 identity makes that partner-class refinement plausible without requiring ASB10 itself to regulate transcription. The optional refinement is deferred here because the exact assayed construct and pair-specific controls remain uninspected; their absence is not asserted. In the absence of contrary evidence or a better-supported finer molecular-function assignment, the source-specific association is retained under the standing project instruction for correct generic binding.

Summary: Nucleus (IDA). In the source immunostaining of human eye tissue, ASB10 shows a distinct nuclear pattern in retinal ganglion cells and inner nuclear layer neurons. Accepted.

Reason: [PMID:22156576 "In the retina, ASB10 was localized to retinal ganglion cells and individual neurons in the inner nuclear layer, where it revealed a distinct nuclear expression pattern."]

Summary: Nucleus (IEA). This electronic row agrees with the immunostaining of human eye tissue, where ASB10 shows a distinct nuclear pattern in retinal ganglion cells and inner nuclear layer neurons. Accepted.

Reason: [PMID:22156576 "In the retina, ASB10 was localized to retinal ganglion cells and individual neurons in the inner nuclear layer, where it revealed a distinct nuclear expression pattern."]

Summary: Cytoplasm (IDA). In the source immunostaining, ASB10 is mainly cytoplasmic and perinuclear in pigmented ciliary epithelium. Accepted.

Reason: [PMID:22156576 "In the ciliary body, ASB10 was mainly observed in the cytoplasm and perinuclear region of pigmented ciliary epithelial cells covering the ciliary processes, with minimal expression in non-pigmented epithelial cells (Fig."]

Summary: Cytoplasm (IEA). This electronic row agrees with immunostaining, where ASB10 is mainly cytoplasmic and perinuclear in pigmented ciliary epithelium. Accepted.

Reason: [PMID:22156576 "In the ciliary body, ASB10 was mainly observed in the cytoplasm and perinuclear region of pigmented ciliary epithelial cells covering the ciliary processes, with minimal expression in non-pigmented epithelial cells (Fig."]

Summary: Cytosol (IEA, ARBA). Consistent with ASB10's cytoplasmic staining; accepted.

Reason: [PMID:22156576 "In the ciliary body, ASB10 was mainly observed in the cytoplasm and perinuclear region of pigmented ciliary epithelial cells covering the ciliary processes, with minimal expression in non-pigmented epithelial cells (Fig."]

Summary: Cytosol (TAS, Reactome R-HSA-8952039: NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex). GOA derives this row from a cytosolic cullin-RING ligase reaction in which ASB10 takes part as an ASB substrate receptor of CRL5. The cached reaction summary does not name ASB10 itself. Accepted.

Reason: [file:reactome/R-HSA-8952039.md "display_name: NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex"]

Summary: Cytosol (TAS, Reactome R-HSA-8952044: AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex). GOA derives this row from a cytosolic cullin-RING ligase reaction in which ASB10 takes part as an ASB substrate receptor of CRL5. The cached reaction summary does not name ASB10 itself. Accepted.

Reason: [file:reactome/R-HSA-8952044.md "display_name: AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex"]

Summary: Cytosol (TAS, Reactome R-HSA-8955241: CAND1 binds cytosolic CRL E3 ubiquitin ligases). GOA derives this row from a cytosolic cullin-RING ligase reaction in which ASB10 takes part as an ASB substrate receptor of CRL5. The cached reaction summary does not name ASB10 itself. Accepted.

Reason: [file:reactome/R-HSA-8955241.md "display_name: CAND1 binds cytosolic CRL E3 ubiquitin ligases"]

Summary: Cytosol (TAS, Reactome R-HSA-8955289: COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes). GOA derives this row from a cytosolic cullin-RING ligase reaction in which ASB10 takes part as an ASB substrate receptor of CRL5. The cached reaction summary does not name ASB10 itself. Accepted.

Reason: [file:reactome/R-HSA-8955289.md "display_name: COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes"]

Summary: Cytosol (TAS, Reactome R-HSA-8956040: COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes). GOA derives this row from a cytosolic cullin-RING ligase reaction in which ASB10 takes part as an ASB substrate receptor of CRL5. The cached reaction summary does not name ASB10 itself. Accepted.

Reason: [file:reactome/R-HSA-8956040.md "display_name: COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes"]

Summary: Protein ubiquitination (IEA, UniPathway). ASB10 ubiquitylates TEM8 for degradation in breast cancer cells. Correct but broad; the substrate-receptor activity is captured by the NEW adaptor row. Kept as non-core.

Reason: [PMID:34285210 "ASB10, an estrogen receptor ERα trans-activated E3 ligase, ubiquitylates TEM8 for degradation, and its deficiency in TNBC resulted in a high homeostatic level of TEM8."]

Summary: Intracellular signal transduction (IEA, InterPro SOCS box superfamily). In ASB proteins the SOCS box recruits Elongin B/C and Cullin 5 to form an E3 ligase. ASB10's known roles are substrate ubiquitination (TEM8) and HSP70 stabilization, not a signalling pathway, so the domain-based mapping overstates its role; marked over-annotated.

Reason: [file:human/ASB10/ASB10-uniprot.txt "CC -!- FUNCTION: May be a substrate-recognition component of a SCF-like ECS"] [PMID:34285210 "ASB10, an estrogen receptor ERα trans-activated E3 ligase, ubiquitylates TEM8 for degradation, and its deficiency in TNBC resulted in a high homeostatic level of TEM8."]

Summary: Ubiquitin-like ligase-substrate adaptor activity (NEW, IMP). ASB10, the SOCS-box substrate receptor of an ECS-type E3, ubiquitylates TEM8 for degradation, and ASB10 deficiency in triple-negative breast cancer cells raises TEM8 levels.

Reason: [PMID:34285210 "ASB10, an estrogen receptor ERα trans-activated E3 ligase, ubiquitylates TEM8 for degradation, and its deficiency in TNBC resulted in a high homeostatic level of TEM8."] [file:human/ASB10/ASB10-uniprot.txt "CC -!- FUNCTION: May be a substrate-recognition component of a SCF-like ECS"]

Summary: Cytoplasmic vesicle (NEW, IDA). In primary human trabecular meshwork cells, confocal and structured-illumination microscopy place ASB10 on small vesicles and larger aggresome-like structures. These co-localize with LC3, p62, Rab7 and LAMP1 markers of the autophagy-lysosome pathway, and their number responds to MG132 and to autophagy inhibitors.

Reason: [PMID:23901248 "ASB10 also colocalized with numerous biomarkers of specific autophagic structures: aggresomes (histone deacetylase 6 [HDAC6] and heat shock protein 70 [HSP70]), autophagosomes (light chain 3 [LC3] and p62), amphisomes (Rab7), and lysosomes (lysosomal-associated membrane protein 1 [LAMP1])."] [PMID:23901248 "Treatment of HTM cells with an autophagy activator (MG132) or inhibitors (wortmannin, bafilomycin A1) significantly increased and decreased the number of small ASB10-stained vesicles, respectively."]

Summary: Cul5-RING ubiquitin ligase complex (NEW, ISS from the paralog ASB11). The ASB-family SOCS box is the Elongin B/C-Cullin 5 module, and ASB11 has direct evidence for assembly into CRL5. ASB10 itself has not been co-purified with CUL5, so this is a family-level inference. It records machine-readably the CRL5 membership that the substrate-receptor activity implies.

Reason: [file:human/ASB10/ASB10-uniprot.txt "CC -!- FUNCTION: May be a substrate-recognition component of a SCF-like ECS"] [PMID:34285210 "ASB10, an estrogen receptor ERα trans-activated E3 ligase, ubiquitylates TEM8 for degradation, and its deficiency in TNBC resulted in a high homeostatic level of TEM8."]