ASB11 is an ankyrin repeat and SOCS box protein that serves as the substrate-recognition subunit of a Cullin 5-RING E3 ubiquitin ligase (CRL5(ASB11), with Elongins B/C and RBX2), activated by UBE2F-dependent CUL5 neddylation. It is associated with the endoplasmic reticulum. Its ankyrin repeats bind substrates, including Ribophorin 1 of the oligosaccharyltransferase, the pro-apoptotic BH3-only protein BIK, the small GTPase DIRAS2 and ERLIN1, and its SOCS box links them to Cullin 5 for ubiquitination and proteasomal degradation. During ER stress, XBP1s induces ASB11, and BIK degradation delays apoptosis in the adaptive phase of the unfolded protein response. ASB11 also builds K6-linked chains on the purine-synthesis enzyme PAICS, which recruit UBAP2 to drive purinosome assembly. FIH hydroxylates asparagines in its ankyrin repeats. In zebrafish, Asb11 ubiquitinates DeltaA, promotes Delta-Notch signalling, and keeps neural and muscle progenitors proliferating.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005783 endoplasmic reticulum | IDA PMID:24337577 Protein interaction screening for the ankyrin repeats and su... | ACCEPT | Summary: Endoplasmic reticulum (IDA). ASB11 is an ER-associated ubiquitin ligase, consistent with its ER substrates Ribophorin 1, BIK and ERLIN1. Core location. Reason: [PMID:24337577 "We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex."] [PMID:31387940 "Similar to BIK, ASB11 is an ER-residing protein (Andresen et al."] ORGANELLES check (2026-11-04): direct evidence, and the ER claim holds: the CRL5(ASB11) substrates Ribophorin 1 and BIK are ER membrane proteins, and ER location is central to its ER-stress role, so ACCEPT stands. The paper (abstract only in the cache; PMC3900953 returned no full text) calls ASB11 ER-associated, not integral, and UniProt annotates no transmembrane segment. The hydrophobic N-terminal stretch (about residues 13-41, absent from isoform 3) is a single, unassayed line for membrane insertion, so no ER-membrane sub-compartment row is added; the row stays at the root. Supporting Evidence: PMID:24337577 We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex. PMID:31387940 Similar to BIK, ASB11 is an ER-residing protein (Andresen et al. |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000044 | ACCEPT | Summary: Endoplasmic reticulum (IEA). ASB11 is an ER-associated ubiquitin ligase, consistent with its ER substrates Ribophorin 1, BIK and ERLIN1. Core location. Reason: [file:human/ASB11/ASB11-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum"] [PMID:31387940 "Similar to BIK, ASB11 is an ER-residing protein (Andresen et al."] ORGANELLES check (2026-11-04): the SL-0095 keyword rests on the curated UniProt line tagged ECO:0000269 with PubMed:24337577, the same paper as the IDA row, so the electronic row restates a real experimental ER location and stays ACCEPT. UniProt gives no ER sub-location and no transmembrane feature, so the row stays at the root (see the IDA row for the single unassayed membrane-anchor line). Supporting Evidence: file:human/ASB11/ASB11-uniprot.txt CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum PMID:31387940 Similar to BIK, ASB11 is an ER-residing protein (Andresen et al. |
| GO:0005829 cytosol | IEA GO_REF:0000117 | ACCEPT | Summary: Cytosol (IEA, ARBA). CRL5(ASB11) ubiquitinates the cytosolic purinosome enzyme PAICS, so it acts in the cytosol as well as at the ER. Accepted. Reason: [PMID:37848033 "Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly."] Supporting Evidence: PMID:37848033 Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly. |
| 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 ASB11, which enters through the CRL5 substrate-receptor set. CRL5(ASB11) acts on the cytosolic face: it ubiquitinates the cytosolic purinosome enzyme PAICS as well as ER-anchored substrates. Accepted. Reason: [file:reactome/R-HSA-8952039.md "display_name: NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex"] [PMID:37848033 "Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly."] Supporting Evidence: file:reactome/R-HSA-8952039.md display_name: NEDD8:AcM-UBE2F binds CRL5 E3 ubiquitin ligase complex PMID:37848033 Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly. |
| 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 ASB11, which enters through the CRL5 substrate-receptor set. CRL5(ASB11) acts on the cytosolic face: it ubiquitinates the cytosolic purinosome enzyme PAICS as well as ER-anchored substrates. Accepted. Reason: [file:reactome/R-HSA-8952044.md "display_name: AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex"] [PMID:37848033 "Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly."] Supporting Evidence: file:reactome/R-HSA-8952044.md display_name: AcM-UBE2F transfers NEDD8 to CRL5 E3 ubiquitin ligase complex PMID:37848033 Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly. |
| 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 ASB11, which enters through the CRL5 substrate-receptor set. CRL5(ASB11) acts on the cytosolic face: it ubiquitinates the cytosolic purinosome enzyme PAICS as well as ER-anchored substrates. Accepted. Reason: [file:reactome/R-HSA-8955241.md "display_name: CAND1 binds cytosolic CRL E3 ubiquitin ligases"] [PMID:37848033 "Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly."] Supporting Evidence: file:reactome/R-HSA-8955241.md display_name: CAND1 binds cytosolic CRL E3 ubiquitin ligases PMID:37848033 Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly. |
| 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 ASB11, which enters through the CRL5 substrate-receptor set. CRL5(ASB11) acts on the cytosolic face: it ubiquitinates the cytosolic purinosome enzyme PAICS as well as ER-anchored substrates. Accepted. Reason: [file:reactome/R-HSA-8955289.md "display_name: COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes"] [PMID:37848033 "Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly."] Supporting Evidence: file:reactome/R-HSA-8955289.md display_name: COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes PMID:37848033 Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly. |
| 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 ASB11, which enters through the CRL5 substrate-receptor set. CRL5(ASB11) acts on the cytosolic face: it ubiquitinates the cytosolic purinosome enzyme PAICS as well as ER-anchored substrates. Accepted. Reason: [file:reactome/R-HSA-8956040.md "display_name: COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes"] [PMID:37848033 "Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly."] Supporting Evidence: file:reactome/R-HSA-8956040.md display_name: COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes PMID:37848033 Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly. |
| GO:0016567 protein ubiquitination | IBA GO_REF:0000033 | ACCEPT | Summary: Protein ubiquitination (IBA). Conserved role of ASB-family substrate receptors; ASB11 has direct evidence (Ribophorin 1, BIK, DIRAS2, PAICS). Core process. Reason: [PMID:24337577 "The ankyrin and SOCS (suppressor of cytokine signaling) box (ASB) family of proteins function as the substrate recognition subunit in a subset of Elongin-Cullin-SOCS (ECS) E3 ubiquitin ligases."] [PMID:31387940 "Here, we identify Cul5-ASB11 as the E3 ligase targeting BIK for ubiquitination and degradation."] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000651312 SUPPORTS TRANSFER ASB node seeded by human ASB11 itself (UniProtKB:Q8WXH4) and ASB9 (UniProtKB:Q96DX5). ASB11 has its own IDA ubiquitination evidence (PMID:24337577, PMID:31387940). Supporting Evidence: PMID:24337577 The ankyrin and SOCS (suppressor of cytokine signaling) box (ASB) family of proteins function as the substrate recognition subunit in a subset of Elongin-Cullin-SOCS (ECS) E3 ubiquitin ligases. PMID:31387940 Here, we identify Cul5-ASB11 as the E3 ligase targeting BIK for ubiquitination and degradation. |
| GO:0016567 protein ubiquitination | IDA PMID:24337577 Protein interaction screening for the ankyrin repeats and su... | ACCEPT | Summary: Protein ubiquitination (IDA). ASB11 promotes ubiquitination of Ribophorin 1 as an ER-associated ubiquitin ligase. Core process. Reason: [PMID:24337577 "We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex."] Supporting Evidence: PMID:24337577 We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex. |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000041 | ACCEPT | Summary: Protein ubiquitination (IEA, UniPathway). Matches UniProt's pathway line for ASB11, which rests on the three substrate studies. Accepted. Reason: [file:human/ASB11/ASB11-uniprot.txt "CC -!- FUNCTION: Substrate-recognition component of a cullin-5-RING E3"] [PMID:31387940 "Here, we identify Cul5-ASB11 as the E3 ligase targeting BIK for ubiquitination and degradation."] Supporting Evidence: file:human/ASB11/ASB11-uniprot.txt CC -!- FUNCTION: Substrate-recognition component of a cullin-5-RING E3 PMID:31387940 Here, we identify Cul5-ASB11 as the E3 ligase targeting BIK for ubiquitination and degradation. |
| GO:0030968 endoplasmic reticulum unfolded protein response | IDA PMID:31387940 BIK ubiquitination by the E3 ligase Cul5-ASB11 determines ce... | ACCEPT | Summary: Endoplasmic reticulum unfolded protein response (IDA). XBP1s induces ASB11 during the adaptive phase of the UPR, and ASB11 then ubiquitinates BIK for p97/VCP-assisted proteasomal degradation, delaying apoptosis while cells adapt. ASB11 performs this pro-survival step of the response itself. Accepted. Reason: [PMID:31387940 "ER stress leads to the activation of ASB11 by XBP1s during the adaptive phase of the unfolded protein response, which stimulates BIK ubiquitination, interaction with p97/VCP, and proteolysis."] [PMID:31387940 "These findings support that ER stress–induced and ASB11-mediated BIK degradation plays a pro-survival role to contribute to the adaptive phase of UPR."] Supporting Evidence: PMID:31387940 ER stress leads to the activation of ASB11 by XBP1s during the adaptive phase of the unfolded protein response, which stimulates BIK ubiquitination, interaction with p97/VCP, and proteolysis. PMID:31387940 These findings support that ER stress–induced and ASB11-mediated BIK degradation plays a pro-survival role to contribute to the adaptive phase of UPR. |
| GO:0031466 Cul5-RING ubiquitin ligase complex | IDA PMID:31387940 BIK ubiquitination by the E3 ligase Cul5-ASB11 determines ce... | ACCEPT | Summary: Cul5-RING ubiquitin ligase complex (IDA). ASB11 assembles with Cullin 5, Elongins B/C and RBX2 (ROC2); a reconstituted Cul5-ASB11 complex ubiquitinates BIK in vitro, and UBE2F-driven CUL5 neddylation activates CRL5(ASB11). Core complex. Reason: [PMID:31387940 "In the in vitro ubiquitination assay, BIK ubiquitination was readily detected in the reaction supplemented with a full Cul5-ASB11 complex, including ROC2, Cul5, ElonginB, ElonginC, and ASB11 (Fig."] Supporting Evidence: PMID:31387940 In the in vitro ubiquitination assay, BIK ubiquitination was readily detected in the reaction supplemented with a full Cul5-ASB11 complex, including ROC2, Cul5, ElonginB, ElonginC, and ASB11 (Fig. |
| GO:0031466 Cul5-RING ubiquitin ligase complex | IDA PMID:38574733 The UBE2F-CRL5(ASB11)-DIRAS2 axis is an oncogene and tumor s... | ACCEPT | Summary: Cul5-RING ubiquitin ligase complex (IDA). ASB11 assembles with Cullin 5, Elongins B/C and RBX2 (ROC2); a reconstituted Cul5-ASB11 complex ubiquitinates BIK in vitro, and UBE2F-driven CUL5 neddylation activates CRL5(ASB11). Core complex. Reason: [PMID:38574733 "Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase."] [PMID:31387940 "In the in vitro ubiquitination assay, BIK ubiquitination was readily detected in the reaction supplemented with a full Cul5-ASB11 complex, including ROC2, Cul5, ElonginB, ElonginC, and ASB11 (Fig."] Supporting Evidence: PMID:38574733 Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase. PMID:31387940 In the in vitro ubiquitination assay, BIK ubiquitination was readily detected in the reaction supplemented with a full Cul5-ASB11 complex, including ROC2, Cul5, ElonginB, ElonginC, and ASB11 (Fig. |
| GO:0035556 intracellular signal transduction | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Intracellular signal transduction (IEA, InterPro SOCS box). The SOCS box of ASB proteins is the Elongin BC/Cullin 5-binding module of a ubiquitin-ligase substrate receptor, and the signalling mapping is inherited from the cytokine-signalling SOCS proteins. ASB11 does affect signalling, for example MAPK output through DIRAS2 degradation and Delta-Notch through DeltaA in zebrafish. It does so by degrading signalling components, which is regulation of signalling rather than participation in signal transduction. Marked as over-annotated, matching the repo's treatment of this InterPro mapping. Reason: [PMID:24337577 "The ankyrin and SOCS (suppressor of cytokine signaling) box (ASB) family of proteins function as the substrate recognition subunit in a subset of Elongin-Cullin-SOCS (ECS) E3 ubiquitin ligases."] [PMID:31387940 "We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig."] [PMID:38574733 "Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase."] Supporting Evidence: PMID:24337577 The ankyrin and SOCS (suppressor of cytokine signaling) box (ASB) family of proteins function as the substrate recognition subunit in a subset of Elongin-Cullin-SOCS (ECS) E3 ubiquitin ligases. PMID:31387940 We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig. PMID:38574733 Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:31387940 BIK ubiquitination by the E3 ligase Cul5-ASB11 determines ce... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent protein catabolic process (IDA). ASB11-mediated ubiquitination of BIK (K48-linked) drives its proteasomal degradation, reversed by MG132. DIRAS2 is likewise ubiquitylated by CRL5(ASB11), and ASB11 also promotes ERLIN1 degradation. Core process. Reason: [PMID:31387940 "These findings indicate that ASB11-mediated BIK ubiquitination promotes its proteasomal degradation."] [PMID:31387940 "As to the ubiquitin chain type, ASB11 promoted BIK K48 ubiquitination (Fig."] [PMID:41668292 "Hypoxia impairs factor-inhibiting hypoxia-1 (FIH)-dependent ASB11 hydroxylation, promoting ASB11-mediated ERLIN1 degradation."] Supporting Evidence: PMID:31387940 These findings indicate that ASB11-mediated BIK ubiquitination promotes its proteasomal degradation. PMID:31387940 As to the ubiquitin chain type, ASB11 promoted BIK K48 ubiquitination (Fig. PMID:41668292 Hypoxia impairs factor-inhibiting hypoxia-1 (FIH)-dependent ASB11 hydroxylation, promoting ASB11-mediated ERLIN1 degradation. |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | IDA PMID:38574733 The UBE2F-CRL5(ASB11)-DIRAS2 axis is an oncogene and tumor s... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent protein catabolic process (IDA). ASB11-mediated ubiquitination of BIK (K48-linked) drives its proteasomal degradation, reversed by MG132. DIRAS2 is likewise ubiquitylated by CRL5(ASB11), and ASB11 also promotes ERLIN1 degradation. Core process. Reason: [PMID:38574733 "Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase."] [PMID:31387940 "These findings indicate that ASB11-mediated BIK ubiquitination promotes its proteasomal degradation."] [PMID:31387940 "As to the ubiquitin chain type, ASB11 promoted BIK K48 ubiquitination (Fig."] [PMID:41668292 "Hypoxia impairs factor-inhibiting hypoxia-1 (FIH)-dependent ASB11 hydroxylation, promoting ASB11-mediated ERLIN1 degradation."] Supporting Evidence: PMID:38574733 Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase. PMID:31387940 These findings indicate that ASB11-mediated BIK ubiquitination promotes its proteasomal degradation. PMID:31387940 As to the ubiquitin chain type, ASB11 promoted BIK K48 ubiquitination (Fig. PMID:41668292 Hypoxia impairs factor-inhibiting hypoxia-1 (FIH)-dependent ASB11 hydroxylation, promoting ASB11-mediated ERLIN1 degradation. |
| GO:0045732 positive regulation of protein catabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Positive regulation of protein catabolic process (IBA). ASB11 promotes turnover of its substrates, but it does so by performing the ubiquitination step of their proteasomal degradation, which GO:0043161 captures directly. Correct but indirect; kept as non-core. Reason: [PMID:24337577 "Moreover, expression of ASB11 can increase Ribophorin 1 protein turnover in vivo."] [PMID:31387940 "These findings indicate that ASB11-mediated BIK ubiquitination promotes its proteasomal degradation."] Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000651312 SUPPORTS TRANSFER ASB node; the only seed is ASB9 (UniProtKB:Q96DX5), which targets creatine kinase B for degradation. ASB11 shares the substrate-turnover role (PMID:24337577, PMID:31387940). Supporting Evidence: PMID:24337577 Moreover, expression of ASB11 can increase Ribophorin 1 protein turnover in vivo. PMID:31387940 These findings indicate that ASB11-mediated BIK ubiquitination promotes its proteasomal degradation. |
| GO:0070979 protein K11-linked ubiquitination | IDA PMID:38574733 The UBE2F-CRL5(ASB11)-DIRAS2 axis is an oncogene and tumor s... | UNDECIDED | Summary: Protein K11-linked ubiquitination (IDA, DIRAS2 study). The cached record is abstract-only and does not state the chain type, so the K11 linkage cannot be checked here. Chain type appears substrate-specific: ASB11 builds K48 chains on BIK and K6 chains on PAICS. Chain-linkage terms are deliberately not asserted as NEW, because linkage depends on the substrate and the accepted GO:0016567 already carries the ubiquitination claim; adding them would only be descendants of an existing annotation. Undecided pending the full text. Reason: The cached abstract of PMID:38574733 does not specify the linkage. Other substrates carry other chain types: [PMID:31387940 "As to the ubiquitin chain type, ASB11 promoted BIK K48 ubiquitination (Fig."] [PMID:37848033 "Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly."] Supporting Evidence: PMID:38574733 Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase. PMID:31387940 As to the ubiquitin chain type, ASB11 promoted BIK K48 ubiquitination (Fig. PMID:37848033 Here, we show that K6-polyubiquitination of the DNPS enzyme phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazolesuccinocarboxamide synthetase (PAICS) by cullin-5/ankyrin repeat and SOCS box containing 11 (Cul5/ASB11)-based ubiquitin ligase plays a driving role in purinosome assembly. |
| GO:1990756 ubiquitin-like ligase-substrate adaptor activity | IDA PMID:24337577 Protein interaction screening for the ankyrin repeats and su... | ACCEPT | Summary: Ubiquitin-like ligase-substrate adaptor activity (IDA). ASB11 is the substrate receptor of the CRL5(ASB11) complex: it binds substrates such as Ribophorin 1, BIK and DIRAS2 and recruits them to Cullin 5 through its SOCS box. Endogenous ASB11 binds BIK, purified ASB11 binds BIK directly, and ASB11 knockdown impairs BIK-Cul5 association. Core function. Reason: [PMID:24337577 "We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex."] [PMID:31387940 "These findings are consistent with the adaptor role of ASB11 in recruiting BIK to the CRL5 complex."] [PMID:31387940 "We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig."] Supporting Evidence: PMID:24337577 We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex. PMID:31387940 These findings are consistent with the adaptor role of ASB11 in recruiting BIK to the CRL5 complex. PMID:31387940 We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig. |
| GO:1990756 ubiquitin-like ligase-substrate adaptor activity | IDA PMID:31387940 BIK ubiquitination by the E3 ligase Cul5-ASB11 determines ce... | ACCEPT | Summary: Ubiquitin-like ligase-substrate adaptor activity (IDA). ASB11 is the substrate receptor of the CRL5(ASB11) complex: it binds substrates such as Ribophorin 1, BIK and DIRAS2 and recruits them to Cullin 5 through its SOCS box. Endogenous ASB11 binds BIK, purified ASB11 binds BIK directly, and ASB11 knockdown impairs BIK-Cul5 association. Core function. Reason: [PMID:31387940 "These findings are consistent with the adaptor role of ASB11 in recruiting BIK to the CRL5 complex."] [PMID:31387940 "We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig."] Supporting Evidence: PMID:31387940 These findings are consistent with the adaptor role of ASB11 in recruiting BIK to the CRL5 complex. PMID:31387940 We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig. |
| GO:1990756 ubiquitin-like ligase-substrate adaptor activity | IDA PMID:38574733 The UBE2F-CRL5(ASB11)-DIRAS2 axis is an oncogene and tumor s... | ACCEPT | Summary: Ubiquitin-like ligase-substrate adaptor activity (IDA). ASB11 is the substrate receptor of the CRL5(ASB11) complex: it binds substrates such as Ribophorin 1, BIK and DIRAS2 and recruits them to Cullin 5 through its SOCS box. Endogenous ASB11 binds BIK, purified ASB11 binds BIK directly, and ASB11 knockdown impairs BIK-Cul5 association. Core function. Reason: [PMID:38574733 "Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase."] [PMID:31387940 "These findings are consistent with the adaptor role of ASB11 in recruiting BIK to the CRL5 complex."] [PMID:31387940 "We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig."] Supporting Evidence: PMID:38574733 Mechanistically, Ube2f deletion inactivates the Mapk-c-Myc signals via blocking ubiquitylation of Diras2, a substrate of CRL5Asb11 E3 ligase. PMID:31387940 These findings are consistent with the adaptor role of ASB11 in recruiting BIK to the CRL5 complex. PMID:31387940 We found that deletion of the SOCS box abolished the capability of ASB11 to promote BIK ubiquitination (Fig. |
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Download this section (compressed HTML)Q: How does ASB11 attach to the ER, and does its hydrophobic N-terminal segment (absent from isoform 3) anchor it there?
Q: What decides whether CRL5(ASB11) builds degradative K48 chains (BIK) or non-degradative K6 chains (PAICS)?
Q: Does human ASB11 ubiquitinate Delta-like ligands and regulate Notch signalling or progenitor maintenance as zebrafish Asb11 does?
Experiment: Map the ER-targeting determinant of ASB11 by fractionation of N-terminal truncations and isoform 3, and test BIK and Ribophorin 1 turnover with each.
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