UFL1 (E3 UFM1-protein ligase 1; also called Maxer, NLBP, RCAD, KIAA0776) is the E3 ligase of the UFM1 (ufmylation) cascade, which catalyzes covalent attachment of the ubiquitin-like modifier UFM1 to substrate lysines. UFL1 is the catalytic component of the UFM1 ribosome E3 ligase (UREL) complex together with its obligate cofactor DDRGK1/UFBP1 and CDK5RAP3; DDRGK1 tethers the complex to the endoplasmic-reticulum membrane. Acting as a non-canonical scaffold-type E3, UFL1 activates the E2 enzyme UFC1 to transfer UFM1 onto substrates. Its principal physiological substrate is the 60S ribosomal protein RPL26/uL24, where mono-ufmylation of RPL26 on ER-bound ribosomes weakens the junction between post-termination or stalled 60S subunits and SEC61 translocons, promoting release and recycling of the large subunit and supporting ribosome-associated protein quality control. UFL1 also drives reticulophagy (ER-phagy) and the response to ER stress through ufmylation of ER proteins such as CYB5R3 and RPN1, participates in the DNA-damage response (ufmylating histone H4 and MRE11 to promote ATM activation), and ufmylates additional substrates including TP53/p53, PD-L1 and PD-1, contributing to protein stabilization and immune regulation. UFL1 acts mainly at the ER membrane but is also recruited to sites of DNA damage in the nucleus.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0071568 UFM1 transferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: UFM1 transferase activity is a near-synonymous description of UFL1's E3 UFM1-ligase activity (transfer of UFM1 to substrate). Reason: UFL1 is the E3 that mediates UFM1 transfer to substrates; this MF term captures that activity, with GO:0061666 (UFM1 ligase activity) being the most precise E3-step term. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0061709 reticulophagy | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: UFL1-mediated ufmylation drives reticulophagy (ER-phagy). Reason: A genuine downstream process of ER ufmylation; non-core relative to the E3 ligase activity. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Involved in reticulophagy in response to endoplasmic reticulum stress |
| GO:0005789 endoplasmic reticulum membrane | IBA GO_REF:0000033 | ACCEPT | Summary: UFL1 acts at the ER membrane as part of the DDRGK1-tethered UREL complex. Reason: ER membrane is the principal site of UFL1 catalytic action. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0034976 response to endoplasmic reticulum stress | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: UFL1-mediated ufmylation functions in the ER stress response. Reason: Valid pathway context; non-core relative to the E3 ligase activity. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Ufmylation in response to endoplasmic reticulum stress |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: UFL1 is recruited to the nucleus/sites of DNA damage; nuclear localization is documented experimentally. Reason: Consistent with UFL1's DNA-damage role at double-strand breaks. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Nucleus |
| GO:0005694 chromosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UFL1 localizes to chromosomes/sites of double-strand breaks during the DNA-damage response. Reason: Documented chromatin localization linked to the DNA-damage role; non-core relative to the principal ER-membrane site of action. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Chromosome |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: ER membrane localization, the principal compartment of UFL1. Reason: Correct compartment; corroborated by experimental evidence. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005829 cytosol | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Cytosolic localization, consistent with UFL1's cytoplasm-facing activity. Reason: Documented cytoplasmic pool; the principal site of action is the ER membrane. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Cytoplasm, cytosol |
| GO:0061666 UFM1 ligase activity | IEA GO_REF:0000002 | ACCEPT | Summary: UFM1 ligase (E3) activity is the core molecular function of UFL1; this electronic annotation is corroborated by extensive direct experimental evidence. Reason: UFL1 is the E3 ligase of the ufmylation cascade; this is its core MF. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0071569 protein ufmylation | IEA GO_REF:0000002 | ACCEPT | Summary: UFL1 is the E3 of protein ufmylation. Reason: Core process annotation for the E3 ligase. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Binary interactome interaction. Bare protein binding is uninformative. Reason: Records a real interaction but the term is uninformative; core MF is UFM1 ligase activity. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:32296183 |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BioPlex affinity-purification interactions. Bare protein binding is uninformative. Reason: Real interactions but uninformative term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:33961781 |
| GO:0005515 protein binding | IPI PMID:37595036 Mechanistic insights into the roles of the UFM1 E3 ligase co... | KEEP AS NON CORE | Summary: Interactions with UREL-complex partners. Bare term uninformative. Reason: Real cascade interactions; non-core under generic term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:37595036 |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: Multimodal cell-maps interaction. Bare protein binding is uninformative. Reason: Real interaction record but uninformative term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:40205054 |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cytoplasmic localization (electronic). Reason: Documented cytoplasmic pool; principal site is the ER membrane. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Cytoplasm, cytosol |
| GO:0010508 positive regulation of autophagy | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: UFL1 promotes autophagy/reticulophagy via ER ufmylation, inferred electronically. Reason: Plausible downstream process; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Involved in reticulophagy in response to endoplasmic reticulum stress |
| GO:0030218 erythrocyte differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Role in erythroid/hematopoietic differentiation inferred by similarity. Reason: Plausible by orthology; downstream developmental role, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Required for hematopoietic stem cell function and hematopoiesis |
| GO:0034976 response to endoplasmic reticulum stress | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ER stress response (electronic), corroborated experimentally. Reason: Valid pathway context; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Ufmylation in response to endoplasmic reticulum stress |
| GO:0043005 neuron projection | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuron-projection localization inferred electronically from the ortholog. Reason: Electronically inferred; peripheral to the core ER-membrane site of action. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0043005 neuron projection cellular_component |
| GO:0050868 negative regulation of T cell activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: UFL1 negatively regulates T-cell activation via ufmylation/stabilization of PD-1, inferred electronically and shown experimentally. Reason: Documented immune-regulatory role; downstream, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Acts as a negative regulator of T-cell activation by mediating ufmylation and stabilization of PDCD1/PD-1 |
| GO:0060218 hematopoietic stem cell differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Role in hematopoietic stem cell function inferred by similarity. Reason: Plausible by orthology; downstream developmental role, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Required for hematopoietic stem cell function and hematopoiesis |
| GO:0050821 protein stabilization | IDA PMID:32807901 UFMylation maintains tumour suppressor p53 stability by anta... | KEEP AS NON CORE | Summary: UFL1-mediated ufmylation of TP53/p53 stabilizes it by antagonizing its ubiquitination. Reason: A documented substrate-specific stabilization effect; downstream of the E3 activity, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Mediates ufmylation of TP53/p53, promoting its stability |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | ACCEPT | Summary: Direct (HPA) ER localization. Reason: IDA-supported ER localization consistent with site of action. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005783 endoplasmic reticulum cellular_component ECO:0000314 IDA GO_REF:0000052 |
| GO:0005694 chromosome | EXP PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | KEEP AS NON CORE | Summary: UFL1 localizes to chromatin/double-strand-break sites during the DNA-damage response (histone H4 ufmylation/ATM activation). Reason: Documented DNA-damage-associated localization; non-core relative to the principal ER-membrane site. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt recruited to double-strand break sites following DNA damage |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:20018847 A novel type of E3 ligase for the Ufm1 conjugation system. | ACCEPT | Summary: Experimental ER membrane localization from the paper identifying UFL1 as the UFM1 E3 ligase. Reason: Direct evidence for the principal compartment. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:20164180 A novel LZAP-binding protein, NLBP, inhibits cell invasion. | ACCEPT | Summary: Experimental ER membrane localization (NLBP/UFL1). Reason: Direct evidence for the principal compartment. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:20228063 A novel C53/LZAP-interacting protein regulates stability of ... | ACCEPT | Summary: Experimental ER membrane localization (RCAD/UFL1). Reason: Direct evidence for the principal compartment. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0071569 protein ufmylation | IDA PMID:36121123 A non-canonical scaffold-type E3 ligase complex mediates pro... | ACCEPT | Summary: UFL1 is the E3 mediating ufmylation in the scaffold-type complex. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:1990234 transferase complex | IPI PMID:36121123 A non-canonical scaffold-type E3 ligase complex mediates pro... | ACCEPT | Summary: UFL1 is the catalytic component of the UREL transferase complex. Reason: UFL1 is a bona fide subunit of the UFM1 E3 ligase (transferase) complex. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Catalytic component of the UFM1 ribosome E3 ligase (UREL) complex |
| GO:0005783 endoplasmic reticulum | IDA PMID:37795761 UFMylation of HRD1 regulates endoplasmic reticulum homeostas... | ACCEPT | Summary: UFL1 acts at the ER (HRD1 ufmylation study). Reason: Direct evidence for the site of action. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0006974 DNA damage response | IDA PMID:32807901 UFMylation maintains tumour suppressor p53 stability by anta... | KEEP AS NON CORE | Summary: UFL1 participates in the DNA-damage response (p53 stabilization context). Reason: A genuine but downstream role of UFL1's ufmylation activity; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Also involved in the response to DNA damage |
| GO:0061666 UFM1 ligase activity | IDA PMID:32807901 UFMylation maintains tumour suppressor p53 stability by anta... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (ufmylation of p53). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0061666 UFM1 ligase activity | IDA PMID:35753586 P4HB UFMylation regulates mitochondrial function and oxidati... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (ufmylation of P4HB). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0061666 UFM1 ligase activity | IDA PMID:37795761 UFMylation of HRD1 regulates endoplasmic reticulum homeostas... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (ufmylation of HRD1/SYVN1). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0071569 protein ufmylation | IDA PMID:32807901 UFMylation maintains tumour suppressor p53 stability by anta... | ACCEPT | Summary: UFL1 ufmylates p53. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Mediates ufmylation of TP53/p53, promoting its stability |
| GO:0071569 protein ufmylation | IDA PMID:35753586 P4HB UFMylation regulates mitochondrial function and oxidati... | ACCEPT | Summary: UFL1 ufmylates P4HB. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0071569 protein ufmylation | IDA PMID:37795761 UFMylation of HRD1 regulates endoplasmic reticulum homeostas... | ACCEPT | Summary: UFL1 ufmylates HRD1/SYVN1. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SYVN1/HRD1 |
| GO:0002841 negative regulation of T cell mediated immune response to tumor cell | IDA PMID:38377992 UFL1 ablation in T cells suppresses PD-1 UFMylation to enhan... | KEEP AS NON CORE | Summary: UFL1 ufmylates/stabilizes PD-1, suppressing anti-tumor T-cell immunity. Reason: A documented immune-regulatory role downstream of the E3 activity; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Acts as a negative regulator of T-cell activation by mediating ufmylation and stabilization of PDCD1/PD-1 |
| GO:0050821 protein stabilization | IDA PMID:38377992 UFL1 ablation in T cells suppresses PD-1 UFMylation to enhan... | KEEP AS NON CORE | Summary: UFL1 ufmylation stabilizes PD-1. Reason: Substrate-specific stabilization downstream of the E3 activity; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt mediating ufmylation and stabilization of PDCD1/PD-1 |
| GO:0050868 negative regulation of T cell activation | IDA PMID:38377992 UFL1 ablation in T cells suppresses PD-1 UFMylation to enhan... | KEEP AS NON CORE | Summary: UFL1 negatively regulates T-cell activation via PD-1 ufmylation. Reason: Documented immune-regulatory role; downstream, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Acts as a negative regulator of T-cell activation by mediating ufmylation and stabilization of PDCD1/PD-1 |
| GO:0061666 UFM1 ligase activity | IDA PMID:36893266 Dysregulation of PD-L1 by UFMylation imparts tumor immune ev... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (ufmylation of PD-L1/CD274). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt CD274/PD-L1 |
| GO:0061666 UFM1 ligase activity | IDA PMID:38377992 UFL1 ablation in T cells suppresses PD-1 UFMylation to enhan... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (ufmylation of PD-1/PDCD1). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt PDCD1/PD-1 |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:36543799 The UFM1 system regulates ER-phagy through the ufmylation of... | ACCEPT | Summary: UFL1 acts at the ER membrane within UREL (CYB5R3/ER-phagy study). Reason: Direct evidence for the site of action. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0045732 positive regulation of protein catabolic process | IDA PMID:36543799 The UFM1 system regulates ER-phagy through the ufmylation of... | KEEP AS NON CORE | Summary: UFL1-mediated ufmylation promotes lysosomal degradation of ufmylated ER proteins (reticulophagy). Reason: Downstream consequence of ER ufmylation; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt thereby promoting lysosomal degradation of ufmylated proteins |
| GO:0061666 UFM1 ligase activity | IDA PMID:36543799 The UFM1 system regulates ER-phagy through the ufmylation of... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (ufmylation of CYB5R3). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0061666 UFM1 ligase activity | IMP PMID:37036982 RPL26/uL24 UFMylation is essential for ribosome-associated q... | ACCEPT | Summary: Functional evidence for UFL1 UFM1 ligase activity in ER ribosome-associated quality control (RPL26 ufmylation). Reason: Direct functional support for the core E3 ligase activity. Supporting Evidence: PMID:37036982 RQC-dependent degradation of ER-APs strictly requires conjugation of the |
| GO:0061666 UFM1 ligase activity | IDA PMID:37595036 Mechanistic insights into the roles of the UFM1 E3 ligase co... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity in the mechanistic UREL study. Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0071569 protein ufmylation | IDA PMID:36543799 The UFM1 system regulates ER-phagy through the ufmylation of... | ACCEPT | Summary: UFL1 ufmylates CYB5R3. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0071569 protein ufmylation | IMP PMID:37036982 RPL26/uL24 UFMylation is essential for ribosome-associated q... | ACCEPT | Summary: UFL1 required for RPL26 ufmylation in ER-RQC. Reason: Functional evidence for the core process. Supporting Evidence: PMID:37036982 UFMylation of translocon-bound 60S subunits modulates the RTJ |
| GO:0071569 protein ufmylation | IDA PMID:37595036 Mechanistic insights into the roles of the UFM1 E3 ligase co... | ACCEPT | Summary: UFL1 mediates ufmylation in the mechanistic UREL study. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0072344 rescue of stalled cytosolic ribosome | IMP PMID:37036982 RPL26/uL24 UFMylation is essential for ribosome-associated q... | ACCEPT | Summary: UFL1, via RPL26 ufmylation, contributes to release/recycling of stalled 60S ribosomes at the ER, supporting ribosome-associated quality control. This is the major biological process of UFL1. Reason: A core physiological role of UFL1 ufmylation - ribosome recycling/RQC at the ER-translocon junction. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt plays a key role in ribosome recycling by catalyzing mono-ufmylation of RPL26/uL24 subunit of the 60S ribosome |
| GO:0072344 rescue of stalled cytosolic ribosome | IDA PMID:37595036 Mechanistic insights into the roles of the UFM1 E3 ligase co... | ACCEPT | Summary: UFL1 contributes to ribosome recycling/RQC via RPL26 ufmylation. Reason: Core physiological role of UFL1 ufmylation. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt plays a key role in ribosome recycling by catalyzing mono-ufmylation of RPL26/uL24 subunit of the 60S ribosome |
| GO:0140501 positive regulation of reticulophagy | IDA PMID:36543799 The UFM1 system regulates ER-phagy through the ufmylation of... | KEEP AS NON CORE | Summary: UFL1-mediated ufmylation positively regulates reticulophagy. Reason: Valid downstream process; non-core relative to the E3 activity. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Involved in reticulophagy in response to endoplasmic reticulum stress |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:38383785 UFM1 E3 ligase promotes recycling of 60S ribosomal subunits ... | ACCEPT | Summary: UFL1 acts at the ER membrane within the UREL-60S complex. Reason: Direct structural evidence for the site of action. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:38383789 The UFM1 E3 ligase recognizes and releases 60S ribosomes fro... | ACCEPT | Summary: UFL1 acts at the ER membrane within the UREL-60S complex. Reason: Direct structural evidence for the site of action. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0032790 ribosome disassembly | IDA PMID:38383785 UFM1 E3 ligase promotes recycling of 60S ribosomal subunits ... | KEEP AS NON CORE | Summary: UFL1-mediated RPL26 ufmylation promotes release/dissociation of 60S from the ER translocon. Reason: Genuine role in 60S release/recycling; captured as downstream process, non-core relative to the E3 MF. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt promoting release and recycling of the large ribosomal subunit |
| GO:0032790 ribosome disassembly | IDA PMID:38383789 The UFM1 E3 ligase recognizes and releases 60S ribosomes fro... | KEEP AS NON CORE | Summary: UFL1-mediated RPL26 ufmylation promotes 60S release from the ER translocon. Reason: Genuine role in 60S release/recycling; downstream process, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt promoting release and recycling of the large ribosomal subunit |
| GO:0061666 UFM1 ligase activity | IDA PMID:30626644 Ribosomal protein RPL26 is the principal target of UFMylatio... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (RPL26 is the principal target). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: PMID:30626644 Ribosomal protein RPL26 is the principal target of UFMylation |
| GO:0061666 UFM1 ligase activity | IDA PMID:36121123 A non-canonical scaffold-type E3 ligase complex mediates pro... | ACCEPT | Summary: UFL1 acts as a non-canonical scaffold-type E3, activating UFC1 to transfer UFM1. Reason: Direct mechanistic support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0061666 UFM1 ligase activity | IDA PMID:38383785 UFM1 E3 ligase promotes recycling of 60S ribosomal subunits ... | ACCEPT | Summary: Structural/functional evidence for UFL1 E3 ligase activity within the UREL-60S complex. Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0061666 UFM1 ligase activity | IDA PMID:38383789 The UFM1 E3 ligase recognizes and releases 60S ribosomes fro... | ACCEPT | Summary: Structural evidence for UFL1 E3 ligase activity in the UREL-60S complex. Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: PMID:38383789 the ubiquitin-like protein UFM1 on the 60S ribosomal subunit protein RPL26 |
| GO:0071569 protein ufmylation | IDA PMID:30626644 Ribosomal protein RPL26 is the principal target of UFMylatio... | ACCEPT | Summary: UFL1 mediates ufmylation; RPL26 is the principal target. Reason: Direct evidence for the core process. Supporting Evidence: PMID:30626644 Ribosomal protein RPL26 is the principal target of UFMylation |
| GO:0071569 protein ufmylation | IDA PMID:38383785 UFM1 E3 ligase promotes recycling of 60S ribosomal subunits ... | ACCEPT | Summary: UFL1 mediates RPL26 ufmylation in the UREL-60S complex. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0071569 protein ufmylation | IDA PMID:38383789 The UFM1 E3 ligase recognizes and releases 60S ribosomes fro... | ACCEPT | Summary: UFL1 mediates RPL26 ufmylation in the UREL-60S complex. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0072344 rescue of stalled cytosolic ribosome | IDA PMID:38383785 UFM1 E3 ligase promotes recycling of 60S ribosomal subunits ... | ACCEPT | Summary: UFL1, via RPL26 ufmylation, contributes to release/recycling of stalled 60S ribosomes at the ER. Reason: Core physiological role of UFL1 ufmylation (ribosome recycling/RQC). Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt plays a key role in ribosome recycling by catalyzing mono-ufmylation of RPL26/uL24 subunit of the 60S ribosome |
| GO:0072344 rescue of stalled cytosolic ribosome | IDA PMID:38383789 The UFM1 E3 ligase recognizes and releases 60S ribosomes fro... | ACCEPT | Summary: UFL1, via RPL26 ufmylation, contributes to release/recycling of stalled 60S ribosomes from the ER translocon. Reason: Core physiological role of UFL1 ufmylation (ribosome recycling/RQC). Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt promoting release and recycling of the large ribosomal subunit |
| GO:0006974 DNA damage response | IDA PMID:30783677 MRE11 UFMylation promotes ATM activation. | KEEP AS NON CORE | Summary: UFL1 ufmylates MRE11 to promote ATM activation in the DNA-damage response. Reason: A genuine but downstream role of UFL1's ufmylation activity; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt mediates monoufmylation of histone H4 and ufmylation of MRE11 |
| GO:0061666 UFM1 ligase activity | IDA PMID:30783677 MRE11 UFMylation promotes ATM activation. | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (ufmylation of MRE11). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt ufmylation of MRE11 |
| GO:0005741 mitochondrial outer membrane | IDA PMID:20164180 A novel LZAP-binding protein, NLBP, inhibits cell invasion. | MARK AS OVER ANNOTATED | Summary: A reported mitochondrial-outer-membrane localization; UFL1's principal and best-supported site of action is the ER membrane, and this localization is not central to its function. Reason: An isolated localization claim at odds with the extensive evidence for ER-membrane action; likely peripheral or context-specific. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005741 mitochondrial outer membrane cellular_component ECO:0000314 IDA PMID:20164180 |
| GO:0000077 DNA damage checkpoint signaling | IDA PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | KEEP AS NON CORE | Summary: UFL1 promotes ATM activation (a DNA-damage checkpoint kinase) via histone H4 ufmylation. Reason: A documented downstream signaling role of UFL1 ufmylation; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt mediates monoufmylation of histone H4 |
| GO:0005515 protein binding | IPI PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | KEEP AS NON CORE | Summary: Interaction with NBN/UFC1 in the histone H4 ufmylation/ATM study. Bare term uninformative. Reason: Real interactions (including cascade partner UFC1); non-core under generic term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:30886146 |
| GO:0005515 protein binding | IPI PMID:32160526 A genome-wide ER-phagy screen highlights key roles of mitoch... | KEEP AS NON CORE | Summary: Interaction with DDRGK1 in the ER-phagy screen. Bare term uninformative. Reason: Real cascade interaction; non-core under generic term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:32160526 |
| GO:0005634 nucleus | IDA PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | ACCEPT | Summary: Direct nuclear localization during the DNA-damage response. Reason: Direct evidence for nuclear localization linked to UFL1's DNA-damage role. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Nucleus |
| GO:0005737 cytoplasm | IDA PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | KEEP AS NON CORE | Summary: Direct cytoplasmic localization. Reason: Documented cytoplasmic pool; principal site is the ER membrane. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Cytoplasm, cytosol |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:32160526 A genome-wide ER-phagy screen highlights key roles of mitoch... | ACCEPT | Summary: ER membrane localization from the ER-phagy screen. Reason: Direct evidence for the principal compartment. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0010508 positive regulation of autophagy | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Positive regulation of autophagy/reticulophagy transferred from ortholog. Reason: Plausible by orthology; downstream process, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Involved in reticulophagy in response to endoplasmic reticulum stress |
| GO:0019901 protein kinase binding | IPI PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | KEEP AS NON CORE | Summary: UFL1 binds the protein kinase ATM (and is phosphorylated by it) in the DNA-damage response. Reason: A real, specific protein-kinase interaction underlying the DNA-damage role; informative but non-core relative to the E3 ligase activity. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Phosphorylated at Ser-462 by ATM |
| GO:0030218 erythrocyte differentiation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Erythroid differentiation role transferred from ortholog. Reason: Plausible by orthology; downstream developmental role, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Required for hematopoietic stem cell function and hematopoiesis |
| GO:0034976 response to endoplasmic reticulum stress | IDA PMID:32160526 A genome-wide ER-phagy screen highlights key roles of mitoch... | KEEP AS NON CORE | Summary: UFL1 functions in the ER stress response. Reason: Valid pathway context; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Ufmylation in response to endoplasmic reticulum stress |
| GO:0035861 site of double-strand break | IDA PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | KEEP AS NON CORE | Summary: UFL1 is recruited to double-strand-break sites during the DNA-damage response. Reason: Documented DNA-damage-associated localization; non-core relative to the principal ER-membrane site. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt recruited to double-strand break sites following DNA damage |
| GO:0043122 regulation of canonical NF-kappaB signal transduction | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: NF-kappaB regulatory role transferred from ortholog (UFL1/DDRGK1 axis). Reason: Plausible by orthology; downstream signaling role, non-core. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0043122 regulation of canonical NF-kappaB signal transduction biological_process ECO:0000250 ISS GO_REF:0000024 |
| GO:0050727 regulation of inflammatory response | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Inflammatory-response regulation transferred from ortholog. Reason: Plausible by orthology; downstream, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt inflammatory response |
| GO:0060218 hematopoietic stem cell differentiation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Hematopoietic stem cell differentiation transferred from ortholog. Reason: Plausible by orthology; downstream developmental role, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Required for hematopoietic stem cell function and hematopoiesis |
| GO:0061666 UFM1 ligase activity | IDA PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity (histone H4 ufmylation). Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt mediates monoufmylation of histone H4 |
| GO:0061666 UFM1 ligase activity | IDA PMID:32160526 A genome-wide ER-phagy screen highlights key roles of mitoch... | ACCEPT | Summary: Direct evidence of UFL1 UFM1 ligase activity in the ER-phagy context. Reason: Direct support for the core E3 ligase molecular function. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0061709 reticulophagy | IDA PMID:32160526 A genome-wide ER-phagy screen highlights key roles of mitoch... | KEEP AS NON CORE | Summary: UFL1 drives reticulophagy via ER ufmylation. Reason: Valid downstream process; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Involved in reticulophagy in response to endoplasmic reticulum stress |
| GO:0071569 protein ufmylation | IDA PMID:30886146 UFL1 promotes histone H4 ufmylation and ATM activation. | ACCEPT | Summary: UFL1 ufmylates histone H4. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt mediates monoufmylation of histone H4 |
| GO:0071569 protein ufmylation | IDA PMID:32160526 A genome-wide ER-phagy screen highlights key roles of mitoch... | ACCEPT | Summary: UFL1 mediates ufmylation in the ER-phagy context. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:1903895 negative regulation of IRE1-mediated unfolded protein response | IDA PMID:32160526 A genome-wide ER-phagy screen highlights key roles of mitoch... | KEEP AS NON CORE | Summary: UFL1/UREL-dependent ufmylation negatively regulates the IRE1 arm of the UPR (via DDRGK1-IRE1-alpha). Reason: Documented signaling role downstream of ufmylation; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Ufmylation-dependent reticulophagy inhibits the unfolded protein response |
| GO:0061666 UFM1 ligase activity | IDA PMID:20018847 A novel type of E3 ligase for the Ufm1 conjugation system. | ACCEPT | Summary: The founding paper identifying UFL1 as the E3 ligase of the UFM1 system, with catalytic activity demonstrated. Reason: Original direct demonstration of the core E3 UFM1 ligase activity. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0032991 protein-containing complex | IDA PMID:20531390 Suppression of the novel ER protein Maxer by mutant ataxin-1... | KEEP AS NON CORE | Summary: UFL1 (Maxer) is part of an ER protein complex; more specifically the UREL complex. Reason: A generic complex-membership term; the specific and informative term is the UREL transferase complex. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0032991 protein-containing complex cellular_component ECO:0000314 IDA PMID:20531390 |
| GO:0001649 osteoblast differentiation | HDA PMID:16210410 Differential expression profiling of membrane proteins by qu... | KEEP AS NON CORE | Summary: From a membrane-proteomics differentiation study; an HDA association not central to UFL1's defined function. Reason: High-throughput association of uncertain functional relevance; non-core. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0001649 osteoblast differentiation biological_process ECO:0007005 HDA PMID:16210410 |
| GO:0016020 membrane | HDA PMID:16210410 Differential expression profiling of membrane proteins by qu... | KEEP AS NON CORE | Summary: Membrane association from proteomics; consistent with UFL1's ER-membrane localization but non-specific. Reason: Generic membrane term; the specific compartment is the ER membrane. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:1990592 protein K69-linked ufmylation | IDA PMID:25219498 Modification of ASC1 by UFM1 is crucial for ERΞ± transactivat... | KEEP AS NON CORE | Summary: UFL1 mediates ufmylation including K69-linked UFM1 chains. Reason: Specific chain-linkage sub-aspect of ufmylation; narrow process annotation. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:1990592 protein K69-linked ufmylation biological_process ECO:0000314 IDA PMID:25219498 |
| GO:0005515 protein binding | IPI PMID:20228063 A novel C53/LZAP-interacting protein regulates stability of ... | KEEP AS NON CORE | Summary: Interaction with CDK5RAP3/DDRGK1 (RCAD study). Bare term uninformative. Reason: Real cascade interactions; non-core under generic term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:20228063 |
| GO:0033146 regulation of intracellular estrogen receptor signaling pathway | IDA PMID:25219498 Modification of ASC1 by UFM1 is crucial for ERΞ± transactivat... | KEEP AS NON CORE | Summary: UFL1 ufmylates TRIP4/ASC1, affecting ERalpha transactivation. Reason: A specialized signaling role downstream of ufmylation; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription |
| GO:0005515 protein binding | IPI PMID:25219498 Modification of ASC1 by UFM1 is crucial for ERΞ± transactivat... | KEEP AS NON CORE | Summary: Interaction with DDRGK1/TRIP4 (ASC1/ufmylation study). Bare term uninformative. Reason: Real cascade-relevant interactions; non-core under generic term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:25219498 |
| GO:0005783 endoplasmic reticulum | IDA PMID:20531390 Suppression of the novel ER protein Maxer by mutant ataxin-1... | ACCEPT | Summary: ER localization (Maxer/UFL1). Reason: Direct evidence for the principal compartment. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:20531390 Suppression of the novel ER protein Maxer by mutant ataxin-1... | ACCEPT | Summary: ER membrane localization (Maxer/UFL1). Reason: Direct evidence for the principal compartment. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0008284 positive regulation of cell population proliferation | IMP PMID:20531390 Suppression of the novel ER protein Maxer by mutant ataxin-1... | KEEP AS NON CORE | Summary: Effect on cell proliferation in the Maxer study. Reason: Downstream cellular phenotype; non-core. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0008284 positive regulation of cell population proliferation biological_process ECO:0000315 IMP PMID:20531390 |
| GO:0032880 regulation of protein localization | IMP PMID:20531390 Suppression of the novel ER protein Maxer by mutant ataxin-1... | KEEP AS NON CORE | Summary: UFL1 affects protein localization in the Maxer study. Reason: Downstream effect; non-core. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0032880 regulation of protein localization biological_process ECO:0000315 IMP PMID:20531390 |
| GO:0032434 regulation of proteasomal ubiquitin-dependent protein catabolic process | IMP PMID:20228063 A novel C53/LZAP-interacting protein regulates stability of ... | KEEP AS NON CORE | Summary: UFL1 regulates proteasomal degradation (protects CDK5RAP3/itself from ubiquitination). Reason: Downstream effect on protein turnover; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation |
| GO:0034976 response to endoplasmic reticulum stress | IDA PMID:23152784 Transcriptional regulation of the Ufm1 conjugation system in... | KEEP AS NON CORE | Summary: UFL1 is up-regulated by ER stress (thapsigargin) and functions in ER homeostasis. Reason: Valid pathway context; non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Up-regulated by thapsigargin |
| GO:0071569 protein ufmylation | IMP PMID:23152784 Transcriptional regulation of the Ufm1 conjugation system in... | ACCEPT | Summary: UFL1 is part of the UFM1 conjugation system implicated in ER homeostasis. Reason: Supports the core process annotation. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
| GO:0005515 protein binding | IPI PMID:20164180 A novel LZAP-binding protein, NLBP, inhibits cell invasion. | KEEP AS NON CORE | Summary: Interaction with CDK5RAP3/LZAP and RELA (NLBP study). Bare term uninformative. Reason: Real interactions (including cascade partner CDK5RAP3); non-core under generic term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:20164180 |
| GO:0031397 negative regulation of protein ubiquitination | IDA PMID:20164180 A novel LZAP-binding protein, NLBP, inhibits cell invasion. | KEEP AS NON CORE | Summary: UFL1 (NLBP) interaction with CDK5RAP3 protects against ubiquitination/degradation. Reason: A documented effect on partner stability; downstream, non-core. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation |
| GO:0005737 cytoplasm | IDA PMID:20164180 A novel LZAP-binding protein, NLBP, inhibits cell invasion. | KEEP AS NON CORE | Summary: Cytoplasmic localization (NLBP/UFL1). Reason: Documented cytoplasmic pool; principal site is the ER membrane. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt Cytoplasm, cytosol |
| GO:0005515 protein binding | IPI PMID:20018847 A novel type of E3 ligase for the Ufm1 conjugation system. | KEEP AS NON CORE | Summary: Interaction with DDRGK1 and UFC1 in the founding UFM1 E3 ligase paper. Bare term uninformative. Reason: Real cascade interactions; non-core under generic term. Supporting Evidence: file:human/UFL1/UFL1-goa.tsv GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:20018847 |
| GO:0005783 endoplasmic reticulum | IDA PMID:20018847 A novel type of E3 ligase for the Ufm1 conjugation system. | ACCEPT | Summary: ER localization from the founding UFM1 E3 ligase paper. Reason: Direct evidence for the principal compartment. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0071569 protein ufmylation | IDA PMID:20018847 A novel type of E3 ligase for the Ufm1 conjugation system. | ACCEPT | Summary: Founding demonstration that UFL1 is the E3 of ufmylation. Reason: Direct evidence for the core process. Supporting Evidence: file:human/UFL1/UFL1-uniprot.txt E3 protein ligase that mediates ufmylation |
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Download this section (compressed HTML)Q: How is UFL1 substrate selectivity determined across its diverse substrates (RPL26, histone H4, MRE11, p53, PD-1/PD-L1, CYB5R3) - is it driven by DDRGK1/CDK5RAP3 adaptors, localization, or post-translational regulation?
Q: Is the reported mitochondrial-outer-membrane localization of UFL1 a genuine functional pool or carryover from ER-mitochondria contact sites?
Q: How does ATM-mediated phosphorylation of UFL1 at Ser-462 mechanistically enhance its ligase activity in the DNA-damage response?
Experiment: Substrate-trapping or proximity-labeling proteomics of catalytically active versus inactive UFL1 across ER-stress, DNA-damage and basal conditions to define context-dependent substrate repertoires.
Experiment: Reconstitute the UREL-60S complex with purified UFL1/DDRGK1/CDK5RAP3 and UFC1 to measure how each subunit and the ATM-phosphorylation site contribute to RPL26 ufmylation and 60S release from SEC61.
Experiment: Separation-of-function UFL1 alleles tested in ER-RQC reporter, reticulophagy, and DNA-damage (ATM activation) assays to determine whether a single catalytic activity underlies all phenotypes.
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